1093:. This separation of myoglobin and hemoglobin allowed for the different functions of the two molecules to arise and develop: myoglobin has more to do with oxygen storage while hemoglobin is tasked with oxygen transport. The α- and β-like globin genes encode the individual subunits of the protein. The predecessors of these genes arose through another duplication event also after the gnathosome common ancestor derived from jawless fish, approximately 450–500 million years ago. Ancestral reconstruction studies suggest that the preduplication ancestor of the α and β genes was a dimer made up of identical globin subunits, which then evolved to assemble into a tetrameric architecture after the duplication. The development of α and β genes created the potential for hemoglobin to be composed of multiple distinct subunits, a physical composition central to hemoglobin's ability to transport oxygen. Having multiple subunits contributes to hemoglobin's ability to bind oxygen cooperatively as well as be regulated allosterically. Subsequently, the α gene also underwent a duplication event to form the
2022:
T2DM results in high levels of glycated hemoglobin in the red blood cells. The normal reference range is approximately 4.0–5.9%. Though difficult to obtain, values less than 7% are recommended for people with T2DM. Levels greater than 9% are associated with poor control of the glycated hemoglobin, and levels greater than 12% are associated with very poor control. Diabetics who keep their glycated hemoglobin levels close to 7% have a much better chance of avoiding the complications that may accompany diabetes (than those whose levels are 8% or higher). In addition, increased glycated of hemoglobin increases its affinity for oxygen, therefore preventing its release at the tissue and inducing a level of hypoxia in extreme cases.
2067:
2282:
1514:(NO) in the globin part of the molecule. This improves oxygen delivery in the periphery and contributes to the control of respiration. NO binds reversibly to a specific cysteine residue in globin; the binding depends on the state (R or T) of the hemoglobin. The resulting S-nitrosylated hemoglobin influences various NO-related activities such as the control of vascular resistance, blood pressure and respiration. NO is not released in the cytoplasm of red blood cells but transported out of them by an anion exchanger called
2565:
2159:
present in red blood cells. Based on the increase in blood CO after the rebreathing period, the hemoglobin mass can be determined through the dilution principle. Although CO gas in large volumes is toxic to humans, the volume of CO used to assess blood volumes corresponds to what would be inhaled when smoking a cigarette. While researchers typically use custom-made rebreathing circuits, the Detalo
Performance from Detalo Health has automated the procedure and made the measurement available to a larger group of users.
1399:
1717:
2633:
62:
661:
1859:, which is exclusively expressed on monocytes or macrophages. Within these cells the hemoglobin molecule is broken up, and the iron gets recycled. This process also produces one molecule of carbon monoxide for every molecule of heme degraded. Heme degradation is the only natural source of carbon monoxide in the human body, and is responsible for the normal blood levels of carbon monoxide in people breathing normal air.
2647:
769:
708:
for women with higher hemoglobin-oxygen affinity when compared to the mortality rate of offspring from women with low hemoglobin-oxygen affinity. While the exact genotype and mechanism by which this occurs is not yet clear, selection is acting on these women's ability to bind oxygen in low partial pressures, which overall allows them to better sustain crucial metabolic processes.
673:
Recent studies of deer mice found mutations in four genes that can account for differences between high- and low-elevation populations. It was found that the genes of the two breeds are "virtually identical—except for those that govern the oxygen-carrying capacity of their hemoglobin. . . . The genetic difference enables highland mice to make more efficient use of their oxygen."
856:, completing the octahedral group of six ligands. This reversible bonding with oxygen is why hemoglobin is so useful for transporting oxygen around the body. Oxygen binds in an "end-on bent" geometry where one oxygen atom binds to Fe and the other protrudes at an angle. When oxygen is not bound, a very weakly bonded water molecule fills the site, forming a distorted
1878:. When the porphyrin ring is broken up, the fragments are normally secreted as a yellow pigment called bilirubin, which is secreted into the intestines as bile. Intestines metabolize bilirubin into urobilinogen. Urobilinogen leaves the body in faeces, in a pigment called stercobilin. Globulin is metabolized into amino acids that are then released into circulation.
1434:). Conversely, when the carbon dioxide levels in the blood decrease (i.e., in the lung capillaries), carbon dioxide and protons are released from hemoglobin, increasing the oxygen affinity of the protein. A reduction in the total binding capacity of hemoglobin to oxygen (i.e. shifting the curve down, not just to the right) due to reduced pH is called the
2855:
half-life is frequently shortened. In these individuals, an alternative test called "fructosamine level" can be used. It measures the degree of glycation (glucose binding) to albumin, the most common blood protein, and reflects average blood glucose levels over the previous 18–21 days, which is the half-life of albumin molecules in the circulation.
787:, and these helices are connected by short non-helical segments. Hydrogen bonds stabilize the helical sections inside this protein, causing attractions within the molecule, which then causes each polypeptide chain to fold into a specific shape. Hemoglobin's quaternary structure comes from its four subunits in roughly a tetrahedral arrangement.
2583:, with the Roman god of war, since the planet is an orange-red, which reminded the ancients of blood. Although the color of the planet is due to iron compounds in combination with oxygen in the Martian soil, it is a common misconception that the iron in hemoglobin and its oxides gives blood its red color. The color is actually due to the
2444:. They were once hypothesized to use the metal vanadium as an oxygen binding prosthetic group. However, although they do contain vanadium by preference, they apparently bind little oxygen, and thus have some other function, which has not been elucidated (sea squirts also contain some hemoglobin). They may act as toxins.
1866:. Increased levels of this chemical are detected in the blood if red blood cells are being destroyed more rapidly than usual. Improperly degraded hemoglobin protein or hemoglobin that has been released from the blood cells too rapidly can clog small blood vessels, especially the delicate blood filtering vessels of the
2516:. It has been suggested that brain hemoglobin in these cells may enable the "storage of oxygen to provide a homeostatic mechanism in anoxic conditions, which is especially important for A9 DA neurons that have an elevated metabolism with a high requirement for energy production". It has been noted further that "A9
2254:(iron in a flat porphyrin support), they are often called hemoglobins, even if their overall tertiary structure is very different from that of vertebrate hemoglobin. In particular, the distinction of "myoglobin" and hemoglobin in lower animals is often impossible, because some of these organisms do not contain
681:. This was also found in hummingbirds that inhabit the Andes. Hummingbirds already expend a lot of energy and thus have high oxygen demands and yet Andean hummingbirds have been found to thrive in high altitudes. Non-synonymous mutations in the hemoglobin gene of multiple species living at high elevations (
1503:, and binds oxygen with greater affinity than adult hemoglobin. This means that the oxygen binding curve for fetal hemoglobin is left-shifted (i.e., a higher percentage of hemoglobin has oxygen bound to it at lower oxygen tension), in comparison to that of adult hemoglobin. As a result, fetal blood in the
2021:
percentage reflects a weighted average of blood glucose levels over the lifetime of red cells, which is approximately 120 days. The levels of glycated hemoglobin are therefore measured in order to monitor the long-term control of the chronic disease of type 2 diabetes mellitus (T2DM). Poor control of
1180:
conformational changes of the hemoglobin protein complex as discussed above; i.e., when one subunit protein in hemoglobin becomes oxygenated, a conformational or structural change in the whole complex is initiated, causing the other subunits to gain an increased affinity for oxygen. As a consequence,
616:
on chromosome 11. The amino acid sequences of the globin subunits usually differ between species, with the difference growing with evolutionary distance. For example, the most common hemoglobin sequences in humans, bonobos and chimpanzees are completely identical, with exactly the same alpha and beta
2370:
for use as synthetic raw material similar to photosynthetic plants. The structures are bright red due to their content of several extraordinarily complex hemoglobins that have up to 144 globin chains, each including associated heme structures. These hemoglobins are remarkable for being able to carry
672:
Variations in hemoglobin sequences, as with other proteins, may be adaptive. For example, hemoglobin has been found to adapt in different ways to the thin air at high altitudes, where lower partial pressure of oxygen diminishes its binding to hemoglobin compared to the higher pressures at sea level.
1349:
oxide occupies a different binding site on the hemoglobin. At tissues, where carbon dioxide concentration is higher, carbon dioxide binds to allosteric site of hemoglobin, facilitating unloading of oxygen from hemoglobin and ultimately its removal from the body after the oxygen has been released to
1164:
side-chain of the histidine residue interacting at the other pole of the iron is pulled toward the porphyrin ring. This interaction forces the plane of the ring sideways toward the outside of the tetramer, and also induces a strain in the protein helix containing the histidine as it moves nearer to
1014:
affinity where, at high partial pressures of oxygen (such as those present in the alveoli), the relaxed (high affinity, R) state is favoured. Inversely, at low partial pressures (such as those present in respiring tissues), the (low affinity, T) tense state is favoured. Additionally, the binding of
707:
Hemoglobin adaptation extends to humans, as well. There is a higher offspring survival rate among
Tibetan women with high oxygen saturation genotypes residing at 4,000 m. Natural selection seems to be the main force working on this gene because the mortality rate of offspring is significantly lower
390:
Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In these organisms, hemoglobins may carry oxygen, or they may transport and regulate other small molecules and ions such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. A variant called
2520:
neurons may be at particular risk of anoxic degeneration since in addition to their high mitochondrial activity they are under intense oxidative stress caused by the production of hydrogen peroxide via autoxidation and/or monoamine oxidase (MAO)-mediated deamination of dopamine and the subsequent
2391:
Found in the muscle tissue of many vertebrates, including humans, it gives muscle tissue a distinct red or dark gray color. It is very similar to hemoglobin in structure and sequence, but is not a tetramer; instead, it is a monomer that lacks cooperative binding. It is used to store oxygen rather
2217:
Hemoglobin can be tracked noninvasively, to build an individual data set tracking the hemoconcentration and hemodilution effects of daily activities for better understanding of sports performance and training. Athletes are often concerned about endurance and intensity of exercise. The sensor uses
1327:, which cannot bind oxygen. Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening. Nitric oxide is capable of converting a small fraction of hemoglobin to methemoglobin in red blood cells. The latter reaction is a remnant activity of the more ancient
468:
published a series of articles in which he described growing hemoglobin crystals by successively diluting red blood cells with a solvent such as pure water, alcohol or ether, followed by slow evaporation of the solvent from the resulting protein solution. Hemoglobin's reversible oxygenation was
2158:
Hemoglobin mass can be measured in humans using the non-radioactive, carbon monoxide (CO) rebreathing technique that has been used for more than 100 years. With this technique, a small volume of pure CO gas is inhaled and rebreathed for a few minutes. During rebreathing, CO binds to hemoglobin
2143:
Laboratory hemoglobin test methods require a blood sample (arterial, venous, or capillary) and analysis on hematology analyzer and CO-oximeter. Additionally, a new noninvasive hemoglobin (SpHb) test method called Pulse CO-Oximetry is also available with comparable accuracy to invasive methods.
1464:
allosteric effect. Hemoglobin in organisms at high altitudes has also adapted such that it has less of an affinity for 2,3-BPG and so the protein will be shifted more towards its R state. In its R state, hemoglobin will bind oxygen more readily, thus allowing organisms to perform the necessary
2854:
level is only useful in individuals who have red blood cells (RBCs) with normal survivals (i.e., normal half-life). In individuals with abnormal RBCs, whether due to abnormal hemoglobin molecules (such as
Hemoglobin S in Sickle Cell Anemia) or RBC membrane defects – or other problems, the RBC
1176:. The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecule, with the first molecules of oxygen bound influencing the shape of the binding sites for the next ones, in a way favorable for binding. This positive cooperative binding is achieved through
2005:. The binding of glucose to amino acids in the hemoglobin takes place spontaneously (without the help of an enzyme) in many proteins, and is not known to serve a useful purpose. However, as the concentration of glucose in the blood increases, the percentage of Hb A that turns into Hb A
1244:
groups in the globin protein to form an S-nitrosothiol, which dissociates into free nitric oxide and thiol again, as the hemoglobin releases oxygen from its heme site. This nitric oxide transport to peripheral tissues is hypothesized to assist oxygen transport in tissues, by releasing
1144:. For example, in the upper-left of the four hemes shown, oxygen binds at the left of the iron atom shown in the upper-left of diagram. This causes the iron atom to move backward into the heme that holds it (the iron moves upward as it binds oxygen, in this illustration), tugging the
2133:
If the concentration is below normal, this is called anemia. Anemias are classified by the size of red blood cells, the cells that contain hemoglobin in vertebrates. The anemia is called "microcytic" if red cells are small, "macrocytic" if they are large, and "normocytic" otherwise.
1265:, and incomplete combustion in furnaces). CO competes with oxygen at the heme binding site. Hemoglobin's binding affinity for CO is 250 times greater than its affinity for oxygen, Since carbon monoxide is a colorless, odorless and tasteless gas, and poses a potentially fatal threat,
1418:). Hemoglobin can bind protons and carbon dioxide, which causes a conformational change in the protein and facilitates the release of oxygen. Protons bind at various places on the protein, while carbon dioxide binds at the α-amino group. Carbon dioxide binds to hemoglobin and forms
431:
1168:
As oxygen binds to one monomer of hemoglobin, the tetramer's conformation shifts from the T (tense) state to the R (relaxed) state. This shift promotes the binding of oxygen to the remaining three monomers' heme groups, thus saturating the hemoglobin molecule with oxygen.
1015:
oxygen to the iron(II) heme pulls the iron into the plane of the porphyrin ring, causing a slight conformational shift. The shift encourages oxygen to bind to the three remaining heme units within hemoglobin (thus, oxygen binding is cooperative).
457:=number of iron atoms per hemoglobin molecule, now known to be 4), the first determination of a protein's molecular mass. This "hasty conclusion" drew ridicule from colleagues who could not believe that any molecule could be so large. However,
1480:. These bind to a phosphate "pocket" on the fish hemoglobin molecule, which stabilizes the tense state and therefore decreases oxygen affinity. GTP reduces hemoglobin oxygen affinity much more than ATP, which is thought to be due to an extra
2270:). In all these groups, heme/globin-containing molecules (even monomeric globin ones) that deal with gas-binding are referred to as oxyhemoglobins. In addition to dealing with transport and sensing of oxygen, they may also deal with NO, CO
2106:/L. 1 g/dL equals about 0.6206 mmol/L, although the latter units are not used as often due to uncertainty regarding the polymeric state of the molecule. This conversion factor, using the single globin unit molecular weight of 16,000
2140:, the proportion of blood volume occupied by red blood cells, is typically about three times the hemoglobin concentration measured in g/dL. For example, if the hemoglobin is measured at 17 g/dL, that compares with a hematocrit of 51%.
2458:, it is a giant free-floating blood protein containing many dozens—possibly hundreds—of iron- and heme-bearing protein subunits bound together into a single protein complex with a molecular mass greater than 3.5 million daltons.
2590:
of hemoglobin to which the iron is bound, not the iron itself, although the ligation and redox state of the iron can influence the pi to pi* or n to pi* electronic transitions of the porphyrin and hence its optical characteristics.
2218:
light-emitting diodes that emit red and infrared light through the tissue to a light detector, which then sends a signal to a processor to calculate the absorption of light by the hemoglobin protein. This sensor is similar to a
1165:
the iron atom. This strain is transmitted to the remaining three monomers in the tetramer, where it induces a similar conformational change in the other heme sites such that binding of oxygen to these sites becomes easier.
2151:. NIRS can be used both on the head and on muscles. This technique is often used for research in e.g. elite sports training, ergonomics, rehabilitation, patient monitoring, neonatal research, functional brain monitoring,
448:
In 1825, Johann
Friedrich Engelhart discovered that the ratio of iron to protein is identical in the hemoglobins of several species. From the known atomic mass of iron, he calculated the molecular mass of hemoglobin to
2110:, is more common for hemoglobin concentration in blood. For MCHC (mean corpuscular hemoglobin concentration) the conversion factor 0.155, which uses the tetramer weight of 64,500 Da, is more common. Normal levels are:
882:
ion, thus iron must exist in the +2 oxidation state to bind oxygen. If superoxide ion associated to Fe is protonated, the hemoglobin iron will remain oxidized and incapable of binding oxygen. In such cases, the enzyme
5642:
Rutjes, H. A.; Nieveen, M. C.; Weber, R. E.; Witte, F.; Van den
Thillart, G. E. E. J. M. (20 June 2007). "Multiple strategies of Lake Victoria cichlids to cope with lifelong hypoxia include hemoglobin switching".
1782:) – A variant form of hemoglobin found in people with sickle cell disease. There is a variation in the β-chain gene, causing a change in the properties of hemoglobin, which results in sickling of red blood cells.
5205:
Pillai, Arvind S.; Chandler, Shane A.; Liu, Yang; Signore, Anthony V.; Cortez-Romero, Carlos R.; Benesch, Justin L. P.; Laganowsky, Arthur; Storz, Jay F.; Hochberg, Georg K. A.; Thornton, Joseph W. (May 2020).
2402:
The second most common oxygen-transporting protein found in nature, it is found in the blood of many arthropods and molluscs. Uses copper prosthetic groups instead of iron heme groups and is blue in color when
3323:
3783:
Perutz, M.F.; Rossmann, M.G.; Cullis, A.F.; Muirhead, H.; Will, G.; North, A.C.T. (1960). "Structure of haemoglobin: a three-dimensional
Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis".
3587:
Letters from Dr. Withering, ... Dr. Ewart, ... Dr. Thorton ... and Dr. Biggs ... together with some other papers, supplementary to two publications on asthma, consumption, fever, and other diseases, by T.
2468:
In leguminous plants, such as alfalfa or soybeans, the nitrogen fixing bacteria in the roots are protected from oxygen by this iron heme containing oxygen-binding protein. The specific enzyme protected is
3616:
Considerations on the
Medicinal Use, and on the Production of Factitious Airs: Part I. By Thomas Beddoes, M.D. Part II. By James Watt, Engineer; "Part 1, section 2, "Of the breathing of man and familiar
7334:
5543:
It is important to note that in the setting of carboxyhemoglobinemia, it is not a reduction in oxygen-carrying capacity that causes pathology, but an impaired delivery of bound oxygen to target tissues.
863:
Even though carbon dioxide is carried by hemoglobin, it does not compete with oxygen for the iron-binding positions but is bound to the amine groups of the protein chains attached to the heme groups.
1913:
Other common causes of low hemoglobin include loss of blood, nutritional deficiency, bone marrow problems, chemotherapy, kidney failure, or abnormal hemoglobin (such as that of sickle-cell disease).
5861:
1851:
reach the end of their life due to aging or defects, they are removed from the circulation by the phagocytic activity of macrophages in the spleen or the liver or hemolyze within the circulation.
7226:
Kneipp J, Balakrishnan G, Chen R, Shen TJ, Sahu SC, Ho NT, Giovannelli JL, Simplaceanu V, Ho C, Spiro T (2005). "Dynamics of allostery in hemoglobin: roles of the penultimate tyrosine H bonds".
6577:"Simultaneous measurements of cerebral oxygenation changes during brain activation by near-infrared spectroscopy and functional magnetic resonance imaging in healthy young and elderly subjects"
1050:
than deoxyhemoglobin, while at 940 nm its absorption is slightly higher. This difference is used for the measurement of the amount of oxygen in a patient's blood by an instrument called a
1315:(Fe) oxidation state to support oxygen and other gases' binding and transport (it temporarily switches to ferric during the time oxygen is bound, as explained above). Initial oxidation to the
1101:
genes. These further duplications and divergences have created a diverse range of α- and β-like globin genes that are regulated so that certain forms occur at different stages of development.
547:
group. Each heme group contains one iron atom, that can bind one oxygen molecule through ion-induced dipole forces. The most common type of hemoglobin in mammals contains four such subunits.
4260:
Projecto-Garcia, Joana; Natarajan, Chandrasekhar; Moriyama, Hideaki; Weber, Roy E.; Fago, Angela; Cheviron, Zachary A.; Dudley, Robert; McGuire, Jimmy A.; Witt, Christopher C. (2013-12-17).
1117:
1441:
It is necessary for hemoglobin to release the oxygen that it binds; if not, there is no point in binding it. The sigmoidal curve of hemoglobin makes it efficient in binding (taking up O
6713:"The multi-hemoglobin system of the hydrothermal vent tube worm Riftia pachyptila. II. Complete polypeptide chain composition investigated by maximum entropy analysis of mass spectra"
6286:
Frasca, D.; Dahyot-Fizelier, C.; Catherine, K.; Levrat, Q.; Debaene, B.; Mimoz, O. (2011). "Accuracy of a continuous noninvasive hemoglobin monitor in intensive care unit patients*".
2278:
scavenging in environments that must be anaerobic. They may even deal with detoxification of chlorinated materials in a way analogous to heme-containing P450 enzymes and peroxidases.
7140:
Eshaghian, S; Horwich, TB; Fonarow, GC (2006). "An unexpected inverse relationship between HbA1c levels and mortality in patients with diabetes and advanced systolic heart failure".
6152:
5678:
Gronenborn, Angela M.; Clore, G.Marius; Brunori, Maurizio; Giardina, Bruno; Falcioni, Giancarlo; Perutz, Max F. (1984). "Stereochemistry of ATP and GTP bound to fish haemoglobins".
2413:
Some marine invertebrates and a few species of annelid use this iron-containing non-heme protein to carry oxygen in their blood. Appears pink/violet when oxygenated, clear when not.
617:
globin protein chains. Human and gorilla hemoglobin differ in one amino acid in both alpha and beta chains, and these differences grow larger between less closely related species.
2423:
Found in many annelids, it is very similar to erythrocruorin, but the heme group is significantly different in structure. Appears green when deoxygenated and red when oxygenated.
1708:) – In adults Hemoglobin F is restricted to a limited population of red cells called F-cells. However, the level of Hb F can be elevated in persons with sickle-cell disease and
1484:
formed that further stabilizes the tense state. Under hypoxic conditions, the concentration of both ATP and GTP is reduced in fish red blood cells to increase oxygen affinity.
4738:
Van
Beekvelt MC, Colier WN, Wevers RA, Van Engelen BG (2001). "Performance of near-infrared spectroscopy in measuring local O2 consumption and blood flow in skeletal muscle".
7034:
2049:. High hemoglobin levels may also be caused by exposure to high altitudes, smoking, dehydration (artificially by concentrating Hb), advanced lung disease and certain tumors.
464:
Although blood had been known to carry oxygen since at least 1794, the oxygen-carrying property of hemoglobin was described by Hünefeld in 1840. In 1851, German physiologist
3690:
3453:
2295:
The structure of hemoglobins varies across species. Hemoglobin occurs in all kingdoms of organisms, but not in all organisms. Primitive species such as bacteria, protozoa,
6099:
914:
of the tetramer of about 64,000 daltons (64,458 g/mol). Thus, 1 g/dL=0.1551 mmol/L. Hemoglobin A is the most intensively studied of the hemoglobin molecules.
4805:
7331:
4961:"Functional brain mapping by blood oxygenation level-dependent contrast magnetic resonance imaging. A comparison of signal characteristics with a biophysical model"
971:
of the lungs. The oxygen then travels through the blood stream to be dropped off at cells where it is utilized as a terminal electron acceptor in the production of
5781:
4179:
3649:
2371:
oxygen in the presence of sulfide, and even to carry sulfide, without being completely "poisoned" or inhibited by it as hemoglobins in most other species are.
1285:
occur; if the CO concentration is increased to 0.1%, unconsciousness will follow. In heavy smokers, up to 20% of the oxygen-active sites can be blocked by CO.
627:
within a single species, although one sequence is usually "most common" in each species. Many of these mutations cause no disease, but some cause a group of
8717:
1269:
have become commercially available to warn of dangerous levels in residences. When hemoglobin combines with CO, it forms a very bright red compound called
3621:
1931:
Decrease of hemoglobin, with or without an absolute decrease of red blood cells, leads to symptoms of anemia. Anemia has many different causes, although
4852:
8553:
4635:
2575:. The images show the 5-foot (1.5 m) tall sculpture right after installation, after 10 days, and after several months of exposure to the elements.
677:
hemoglobin featured mutations that allowed for oxygen delivery at lower temperatures, thus enabling mammoths to migrate to higher latitudes during the
329:
seventy-fold compared to dissolved oxygen in blood plasma alone. The mammalian hemoglobin molecule can bind and transport up to four oxygen molecules.
3482:
2976:
Sidell, Bruce; Kristin O'Brien (2006). "When bad things happen to good fish: the loss of hemoglobin and myoglobin expression in
Antarctic icefishes".
2127:
Normal values of hemoglobin in the 1st and 3rd trimesters of pregnant women must be at least 11 g/dL and at least 10.5 g/dL during the 2nd trimester.
693:(IHP), a molecule found in birds that has a similar role as 2,3-BPG in humans; this results in the ability to bind oxygen in lower partial pressures.
8729:
4197:
2194:
proportion of 6.0% or less show good long-term glucose control, while values above 7.0% are elevated. This test is especially useful for diabetics.
844:
atoms in the center of the ring, which all lie in one plane. The heme is bound strongly (covalently) to the globular protein via the N atoms of the
8585:
7385:
1308:
S). All of these bind to iron in heme without changing its oxidation state, but they nevertheless inhibit oxygen-binding, causing grave toxicity.
6575:
Mehagnoul-Schipper DJ, van der Kallen BF, Colier WN, van der Sluijs MC, van Erning LJ, Thijssen HO, Oeseburg B, Hoefnagels WH, Jansen RW (2002).
1006:
at the level of the tissues favor the taut form, which has low oxygen affinity and releases oxygen in the tissues. Conversely, a high pH, low CO
8977:
3911:
Nishi, Hiroshi; Inagi, Reiko; Kato, Hideki; Tanemoto, Masayuki; Kojima, Ichiro; Son, Daisuke; Fujita, Toshiro; Nangaku, Masaomi (August 2008).
2525:. The hemoglobin-derived iron in these cells is not the cause of the post-mortem darkness of these cells (origin of the Latin name, substantia
2201:(fMRI) machine uses the signal from deoxyhemoglobin, which is sensitive to magnetic fields since it is paramagnetic. Combined measurement with
898:, consisting of two α and two β subunits non-covalently bound, each made of 141 and 146 amino acid residues, respectively. This is denoted as α
1456:(2,3-BPG) in the blood is increased, which allows these individuals to deliver a larger amount of oxygen to tissues under conditions of lower
8982:
6189:
3592:
2521:
reaction of accessible ferrous iron to generate highly toxic hydroxyl radicals". This may explain the risk of degeneration of these cells in
1018:
Classically, the iron in oxyhemoglobin is seen as existing in the iron(II) oxidation state. However, the complex of oxygen with heme iron is
1939:
are the most common causes in the
Western world. As absence of iron decreases heme synthesis, red blood cells in iron deficiency anemia are
6149:
6037:
5448:
Jensen, Frank B (2009). "The dual roles of red blood cells in tissue oxygen delivery: oxygen carriers and regulators of local blood flow".
3748:
2610:. The intentional rusting of the initially shiny work of art mirrors hemoglobin's fundamental chemical reaction of oxygen binding to iron.
379:
of the kidney, endometrial cells, cervical cells, and vaginal epithelial cells. In these tissues, hemoglobin absorbs unneeded oxygen as an
6265:
1894:(genetic defects resulting in abnormal structure of the hemoglobin molecule) may cause both. In any case, hemoglobin deficiency decreases
1720:
Gene expression of hemoglobin before and after birth. Also identifies the types of cells and organs in which the gene expression (data on
8929:
5944:
5881:
4500:
6754:"Biochemical and enzymological aspects of the symbiosis between the deep-sea tubeworm Riftia pachyptila and its bacterial endosymbiont"
6218:
4616:
1148:
residue (modeled as a red pentagon on the right of the iron) closer, as it does. This, in turn, pulls on the protein chain holding the
948:
In general, hemoglobin can be saturated with oxygen molecules (oxyhemoglobin), or desaturated with oxygen molecules (deoxyhemoglobin).
878:) (Fe) cannot bind oxygen. In binding, oxygen temporarily and reversibly oxidizes (Fe) to (Fe) while oxygen temporarily turns into the
1026:. Experimental evidence strongly suggests heme iron is in the iron(III) oxidation state in oxyhemoglobin, with the oxygen existing as
8638:
7064:
2230:
A variety of oxygen-transport and -binding proteins exist in organisms throughout the animal and plant kingdoms. Organisms including
4239:
7751:
7030:
6429:
McCully, K. K.; Hamaoka, T. (2000). "Near-infrared spectroscopy: What can it tell us about oxygen saturation in skeletal muscle?".
2946:
Maton, Anthea; Jean Hopkins; Charles William McLaughlin; Susan Johnson; Maryanna Quon Warner; David LaHart; Jill D. Wright (1993).
1921:
3701:
3461:
8967:
5908:
3386:
6690:
4822:
4786:
2492:
Some nonerythroid cells (i.e., cells other than the red blood cell line) contain hemoglobin. In the brain, these include the A9
813:
arrangement. Such a name is given because this arrangement is the same folding motif used in other heme/globin proteins such as
664:
Protein alignment of human hemoglobin proteins, alpha, beta, and delta subunits respectively. The alignments were created using
7872:
6096:
4534:
4156:
2315:
contain very large multisubunit molecules, much larger than those in vertebrates. In particular, chimeric hemoglobins found in
7199:
7178:
7130:
7013:
6953:
5938:
5846:
5757:
5626:
5585:
5500:
4943:
4721:
4528:
4482:
4398:
3261:
3193:
3166:
2957:
2930:
2888:
2198:
840:
bridges) with the iron ion bound in the center. The iron ion, which is the site of oxygen binding, coordinates with the four
4802:
3199:
2190:
proportion represents glucose level in blood averaged over the half-life of red blood cells, is typically ~120 days. An Hb A
8863:
8578:
7378:
5866:
5531:
3134:
1340:
906:. The subunits are structurally similar and about the same size. Each subunit has a molecular weight of about 16,000
852:
residue (also known as the proximal histidine) below the porphyrin ring. A sixth position can reversibly bind oxygen by a
317:(excluding water), and around 35% of the total weight (including water). Hemoglobin has an oxygen-binding capacity of 1.34
8972:
2978:
1010:, or low 2,3 BPG favors the relaxed form, which can better bind oxygen. The partial pressure of the system also affects O
5081:
Goodman, Morris; Moore, G. William; Matsuda, Genji (1975-02-20). "Darwinian evolution in the genealogy of haemoglobin".
4657:
3072:"Equality of the in vivo and in vitro oxygen-binding capacity of hemoglobin in patients with severe respiratory disease"
7822:
7677:
2617:, a sculpture in stainless steel that shows the structure of the hemoglobin molecule. It is displayed in the atrium of
2130:
Dehydration or hyperhydration can greatly influence measured hemoglobin levels. Albumin can indicate hydration status.
921:
molecule is made up of 2 α chains and 2 γ chains. The γ chains are gradually replaced by β chains as the infant grows.
4065:
1768:) – A variant form of hemoglobin, formed by a tetramer of γ chains, which may be present in variants of α thalassemia.
716:
Hemoglobin (Hb) is synthesized in a complex series of steps. The heme part is synthesized in a series of steps in the
8914:
8648:
7220:
5773:
4176:
1046:
of oxyhemoglobin and deoxyhemoglobin differ. The oxyhemoglobin has significantly lower absorption of the 660 nm
8951:
4123:
4094:
2123:
Pregnant women: 11 to 14 g/dL (110 to 140 g/L, or 6.83 to 8.69 mmol/L) (9.5 to 15 usual value during pregnancy)
8875:
6655:"The hemoglobin concentration of Chironomus cf.Plumosus L. (Diptera: Chironomidae) larvae from two lentic habitats"
1984:
1156:
When oxygen binds to the iron complex, it causes the iron atom to move back toward the center of the plane of the
9058:
9043:
9010:
8571:
7371:
7089:
2618:
2483:
A synthetic cobalt-based porphyrin. Coboprotein would appear colorless when oxygenated, but yellow when in veins.
1277:
victims to appear pink in death, instead of white or blue. When inspired air contains CO levels as low as 0.02%,
963:
when oxygen binds to the heme component of the protein hemoglobin in red blood cells. This process occurs in the
1814:) – Another variant due to a variation in the β-chain gene. This variant causes a mild chronic hemolytic anemia.
649:
involves underproduction of normal and sometimes abnormal hemoglobins, through problems and mutations in globin
9053:
8777:
7741:
6248:
6177:
5563:
4881:
2921:
2170:. Measuring it directly would require many samples because blood sugar levels vary widely through the day. Hb A
1895:
6632:
3614:
2342:, these worms contain a population of bacteria constituting half the organism's weight. The bacteria oxidize H
1870:, causing kidney damage. Iron is removed from heme and salvaged for later use, it is stored as hemosiderin or
1422:. This decrease in hemoglobin's affinity for oxygen by the binding of carbon dioxide and acid is known as the
1350:
tissues undergoing metabolism. This increased affinity for carbon dioxide by the venous blood is known as the
571:
which determine the protein's chemical properties and function. The amino acid sequence of any polypeptide is
8904:
8662:
7468:
7345:
6014:
5713:
Weber, Roy E.; Frank B. Jensen (1988). "Functional adaptations in hemoglobins from ectothermic vertebrates".
4848:
2358:. The worms' upper end is a deep-red fan-like structure ("plume"), which extends into the water and absorbs H
1460:. This phenomenon, where molecule Y affects the binding of molecule X to a transport molecule Z, is called a
4632:
2242:
all have hemoglobin-like proteins whose known and predicted roles include the reversible binding of gaseous
2147:
Concentrations of oxy- and deoxyhemoglobin can be measured continuously, regionally and noninvasively using
1994:
at the terminal valine (an alpha aminoacid) of each β chain. The resulting molecule is often referred to as
8899:
7590:
3476:
2206:
2152:
1970:. Other mutations, as discussed at the beginning of the article, are benign and are referred to merely as
1694:) – δ chain synthesis begins late in the third trimester and, in adults, it has a normal range of 1.5–3.5%
704:. These two adaptations reinforce each other and account for birds' remarkable high-altitude performance.
8821:
8787:
8633:
7760:
7709:
7560:
4329:"Higher offspring survival among Tibetan women with high oxygen saturation genotypes residing at 4,000 m"
4201:
2579:
Historically, an association between the color of blood and rust occurs in the association of the planet
1530:
17:
2025:
Elevated levels of hemoglobin are associated with increased numbers or sizes of red blood cells, called
1754:) – A variant form of hemoglobin, formed by a tetramer of β chains, which may be present in variants of
8909:
8760:
7865:
7714:
5606:
3319:"Unexpected expression of alpha- and beta-globin in mesencephalic dopaminergic neurons and glial cells"
2904:
2202:
2148:
1932:
360:
3864:"John Kendrew and myoglobin: Protein structure determination in the 1950s: John Kendrew and Myoglobin"
1916:
The ability of each hemoglobin molecule to carry oxygen is normally modified by altered blood pH or CO
8870:
8667:
7622:
7553:
7534:
7322:
4262:"Repeated elevational transitions in hemoglobin function during the evolution of Andean hummingbirds"
2908:
1925:
1274:
976:
438:
7108:
760:(this hemoglobin-synthetic RNA in fact gives the reticulocyte its reticulated appearance and name).
8747:
7940:
7698:
7565:
7529:
7423:
6893:
Nishi, H.; Inagi, R.; Kato, H.; Tanemoto, M.; Kojima, I.; Son, D.; Fujita, T.; Nangaku, M. (2008).
2030:
1328:
1266:
980:
960:
853:
783:
characteristic of many multi-subunit globular proteins. Most of the amino acids in hemoglobin form
485:
6197:
4731:
3585:
3410:
Weber RE, Vinogradov SN (2001). "Nonvertebrate hemoglobins: functions and molecular adaptations".
2841:
Although other sources can have slightly differing values, such as UK's General Practice Notebook.
1890:, or by decreased ability of each molecule to bind oxygen at the same partial pressure of oxygen.
1402:
The sigmoidal shape of hemoglobin's oxygen-dissociation curve results from cooperative binding of
1042:
Deoxygenated hemoglobin (deoxyhemoglobin) is the form of hemoglobin without the bound oxygen. The
8831:
8643:
8018:
7962:
7731:
7600:
7213:
4959:
Ogawa, S; Menon, R. S.; Tank, D. W.; Kim, S. G.; Merkle, H; Ellermann, J. M.; Ugurbil, K (1993).
4030:"Using the NCBI Genome Databases to Compare the Genes for Human & Chimpanzee Beta Hemoglobin"
1534:
1453:
884:
732:
in the cytosol. Production of Hb continues in the cell throughout its early development from the
461:
confirmed Engelhart's results in 1925 by measuring the osmotic pressure of hemoglobin solutions.
415:
387:. Excessive glucose in the blood can attach to hemoglobin and raise the level of hemoglobin A1c.
7999:
6054:
Madsen, H; Ditzel, J (1984). "Blood-oxygen transport in first trimester of diabetic pregnancy".
6034:
5139:"Gene duplication, genome duplication, and the functional diversification of vertebrate globins"
3643:
2621:'s research centre in Montreal. The sculpture measures about 10 metres × 10 metres × 10 metres.
1886:
Hemoglobin deficiency can be caused either by a decreased amount of hemoglobin molecules, as in
8765:
8657:
8628:
7548:
7495:
7485:
7394:
6456:
Perrey, S. P. (2008). "Non-invasive NIR spectroscopy of human brain function during exercise".
6261:
2522:
1936:
1824:
Hemoglobin SC disease – A compound heterozygous form with one sickle gene and another encoding
1796:) – Another variant due to a variation in the β-chain gene. This variant causes a mild chronic
1477:
1473:
1213:
972:
458:
5926:
5878:
4497:
8962:
8941:
7858:
7736:
7672:
2175:
1236:; this mechanism is thought to account for about 10% of carbon dioxide transport in mammals.
1221:
1209:
1196:
The dynamic mechanism of the cooperativity in hemoglobin and its relation with low-frequency
964:
929:
825:
572:
477:
326:
7850:
6226:
5837:
Coomes, Marguerite W. (2011). "Amino Acid and Heme Metabolism". In Devlin, Thomas M. (ed.).
4613:
2052:
A recent study done in Pondicherry, India, shows its importance in coronary artery disease.
798:
subunits. Each subunit is composed of a protein chain tightly associated with a non-protein
756:
allows further synthesis of Hb until the reticulocyte loses its RNA soon after entering the
9048:
8892:
8858:
8679:
8605:
8143:
8129:
8115:
8101:
7791:
7646:
7610:
7445:
7440:
6806:
6666:
6342:
5359:
5292:
5219:
5150:
5090:
5032:
4972:
4568:
4340:
4273:
3793:
3556:
3332:
2682:
2083:
1955:
is caused by the hemoglobin metabolite bilirubin, and the circulating hemoglobin can cause
1831:
780:
211:
193:
175:
7056:
4116:"HBA1 – Hemoglobin subunit alpha – Pan troglodytes (Chimpanzee) – HBA1 gene & protein"
4087:"HBB – Hemoglobin subunit beta – Pan paniscus (Pygmy chimpanzee) – HBB gene & protein"
1257:
The binding of oxygen is affected by molecules such as carbon monoxide (for example, from
8:
8887:
8742:
8409:
8379:
8303:
7945:
7473:
5677:
5021:"Discovery of the magnetic behavior of hemoglobin: A beginning of bioinorganic chemistry"
4235:
2660:
2595:
2572:
2380:
2070:
A hemoglobin concentration measurement being administered before a blood donation at the
2002:
1971:
1526:
1419:
1233:
1190:
1173:
1043:
642:
638:
624:
337:
275:
8836:
6810:
6670:
6346:
5726:
5363:
5296:
5223:
5154:
5094:
5036:
4976:
4572:
4344:
4327:
Beall, Cynthia M.; Song, Kijoung; Elston, Robert C.; Goldstein, Melvyn C. (2004-09-28).
4277:
3797:
3560:
3336:
2945:
1468:
Animals other than humans use different molecules to bind to hemoglobin and change its O
1085:
Scientists agree that the event that separated myoglobin from hemoglobin occurred after
8782:
8691:
8686:
8393:
8075:
7801:
7796:
7776:
7634:
7510:
7289:
7256:
6986:
6919:
6894:
6682:
6601:
6576:
6526:
Siebenmann, Christoph; Keiser, Stefanie; Robach, Paul; Lundby, Carsten (29 June 2017).
6411:
6363:
6330:
6311:
6079:
5473:
5261:
5248:
5207:
5179:
5138:
5114:
5055:
5020:
4993:
4960:
4763:
4304:
4261:
4057:
4005:
3972:
3945:
3912:
3888:
3863:
3817:
3545:"A critical study of the direct method of measuring the osmotic pressure of hǣmoglobin"
3520:
3503:
3435:
3355:
3318:
3285:
3256:
3101:
3003:
2724:
2718:
2259:
2071:
2038:
1542:
1355:
968:
937:
925:
891:
757:
628:
470:
6399:
5924:
5905:
5323:
5280:
4984:
4447:
4420:
4371:
4328:
3378:
3047:
3022:
332:
Hemoglobin also transports other gases. It carries off some of the body's respiratory
9020:
8793:
8374:
8269:
7839:
7755:
7721:
7523:
7478:
7460:
7294:
7276:
7243:
7216:
7195:
7189:
7174:
7157:
7126:
7009:
6990:
6949:
6943:
6924:
6875:
6834:
6829:
6794:
6775:
6770:
6753:
6734:
6654:
6606:
6557:
6549:
6508:
6473:
6438:
6403:
6368:
6315:
6303:
6244:
6173:
6071:
5988:
5983:
5966:
5934:
5842:
5819:
5802:
Kikuchi, G.; Yoshida, T.; Noguchi, M. (2005). "Heme oxygenase and heme degradation".
5753:
5730:
5695:
5691:
5660:
5622:
5581:
5559:
5523:
5496:
5465:
5430:
5426:
5395:
5390:
5377:
5347:
5328:
5310:
5265:
5253:
5235:
5184:
5166:
5106:
5060:
4998:
4939:
4916:
4911:
4894:
4877:
4826:
4783:
4755:
4701:
4596:
4591:
4556:
4524:
4478:
4452:
4376:
4358:
4309:
4291:
4049:
4010:
3992:
3950:
3932:
3893:
3844:
3809:
3525:
3427:
3360:
3290:
3255:
Saha, D.; Reddy, K. V. R.; Patgaonkar, M.; Ayyar, K.; Bashir, T.; Shroff, A. (2014).
3237:
3189:
3162:
3126:
3093:
3052:
2995:
2953:
2947:
2926:
2884:
2670:
2334:, also called Vestimentifera), which can reach 2.4 meters length and populates ocean
2287:
2205:
shows good correlation with both the oxy- and deoxyhemoglobin signal compared to the
2066:
2046:
2010:
1907:
1818:
1755:
1669:
1636:
1585:
1515:
1270:
1212:, which binds to hemoglobin in a cooperative manner, hemoglobin ligands also include
1172:
In the tetrameric form of normal adult hemoglobin, the binding of oxygen is, thus, a
1059:
87:
6686:
6574:
6544:
6527:
6083:
4767:
4148:
4061:
3439:
3105:
3007:
8919:
8816:
8811:
8754:
8737:
8279:
8238:
8168:
7656:
7605:
7515:
7430:
7284:
7268:
7235:
7149:
6982:
6978:
6914:
6906:
6865:
6824:
6814:
6765:
6724:
6674:
6596:
6588:
6539:
6504:
6500:
6465:
6415:
6395:
6358:
6350:
6295:
6129:
6063:
5978:
5811:
5722:
5687:
5652:
5457:
5422:
5385:
5367:
5318:
5300:
5243:
5227:
5174:
5158:
5118:
5098:
5050:
5040:
4988:
4980:
4906:
4747:
4691:
4586:
4576:
4518:
4442:
4432:
4366:
4348:
4299:
4281:
4041:
4000:
3984:
3940:
3924:
3883:
3875:
3821:
3801:
3756:
3564:
3515:
3419:
3350:
3340:
3280:
3270:
3229:
3083:
3042:
3034:
2987:
2768:
2692:
2607:
2587:
2497:
2326:
One of the most striking occurrences and uses of hemoglobin in organisms is in the
2281:
2251:
2061:
2017:
also runs high. Because of the slow rate of Hb A combination with glucose, the Hb A
1963:
1903:
1891:
1797:
1761:
1709:
1546:
1488:
1301:
1182:
1090:
1027:
918:
911:
799:
795:
633:
540:
484:
determined the molecular structure of hemoglobin. For this work he shared the 1962
364:
7316:
5477:
4895:"Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm"
4718:
4394:
3423:
100:
8704:
8533:
8388:
7834:
7682:
7651:
7349:
7338:
7120:
6299:
6156:
6103:
6041:
5912:
5885:
4809:
4790:
4725:
4639:
4620:
4504:
4183:
3371:
3183:
3156:
3023:"Is hemoglobin an essential structural component of human erythrocyte membranes?"
2652:
2541:
2513:
2505:
2339:
2327:
1852:
1541:, caused by variations in genetics. Some well-known hemoglobin variants, such as
1293:
1258:
1232:(NO). The carbon dioxide is bound to amino groups of the globin proteins to form
1217:
1105:
887:
will be able to eventually reactivate methemoglobin by reducing the iron center.
733:
650:
556:
536:
384:
259:
7272:
6469:
5517:
5162:
4751:
3988:
3233:
3120:
2606:
in 2005, based on the protein's backbone. The sculpture was made from glass and
752:
and many other species. Even after the loss of the nucleus in mammals, residual
645:
was understood at the molecular level. A mostly separate set of diseases called
9015:
8924:
8853:
8674:
8623:
8435:
8430:
7780:
7770:
7627:
7585:
7450:
7103:
6799:
Proceedings of the National Academy of Sciences of the United States of America
5815:
5656:
5352:
Proceedings of the National Academy of Sciences of the United States of America
5285:
Proceedings of the National Academy of Sciences of the United States of America
5281:"Rapid duplication and loss of genes coding for the alpha chains of hemoglobin"
4333:
Proceedings of the National Academy of Sciences of the United States of America
3324:
Proceedings of the National Academy of Sciences of the United States of America
2638:
2553:
2449:
2219:
2087:
2042:
1983:
that are characterized by errors in metabolic pathways of heme synthesis. King
1956:
1848:
1457:
1177:
1070:
1051:
984:
503:
407:
376:
333:
295:
251:
112:
7239:
7153:
6528:"CORP: The assessment of total hemoglobin mass by carbon monoxide rebreathing"
6067:
5600:
5231:
4696:
4679:
3761:
3069:
2564:
2155:, urology (bladder contraction), neurology (Neurovascular coupling) and more.
1398:
396:
9037:
8843:
8826:
8770:
8723:
8540:
8499:
8414:
8221:
8003:
7986:
7925:
7786:
7542:
7455:
7280:
6553:
5381:
5314:
5239:
5170:
4653:
4362:
4295:
4053:
4045:
3996:
3936:
3220:
Epstein, F. H.; Hsia, C. C. W. (1998). "Respiratory Function of Hemoglobin".
3088:
3071:
2876:
2708:
2702:
2549:
2463:
2418:
2335:
2179:
2107:
2034:
1680:
1481:
1359:
1324:
933:
907:
875:
817:. This folding pattern contains a pocket that strongly binds the heme group.
753:
392:
372:
299:
208:
190:
172:
116:
6819:
6729:
6712:
6386:
Madsen, P. L.; Secher, N. H. (1999). "Near-infrared oximetry of the brain".
6134:
6117:
5045:
4581:
4353:
4286:
3345:
1834:– A variant form of hemoglobin that is sometimes viewed in combination with
9005:
8936:
8712:
8528:
8469:
8345:
8331:
8317:
8207:
8182:
7726:
7595:
7577:
7435:
7298:
7247:
7161:
6928:
6910:
6879:
6870:
6853:
6838:
6779:
6610:
6561:
6512:
6477:
6442:
6407:
6354:
6307:
5823:
5664:
5527:
5469:
5413:
Chou KC (1989). "Low-frequency resonance and cooperativity of hemoglobin".
5399:
5372:
5305:
5257:
5188:
5064:
4920:
4759:
4520:
Disorders of Hemoglobin: Genetics, Pathophysiology, and Clinical Management
4380:
4313:
4029:
4014:
3954:
3928:
3897:
3848:
3813:
3569:
3544:
3529:
3431:
3364:
3294:
3130:
3056:
2999:
2530:
2517:
2493:
2026:
1835:
1825:
1803:
1785:
1771:
1736:
1697:
1656:
1623:
1511:
1426:. The Bohr effect favors the T state rather than the R state. (shifts the O
1246:
1237:
1229:
1132:
only as diagrammatic coils, to facilitate visualization into the molecule.
1116:
1074:
1066:
1023:
745:
737:
717:
697:
583:
500:
489:
419:
349:
345:
274:) to the other tissues of the body, where it releases the oxygen to enable
6738:
6372:
6075:
5992:
5967:"Hazards of hypoxemia: How to protect your patient from low oxygen levels"
5734:
5699:
5434:
5332:
5110:
5002:
4705:
4600:
4456:
3478:
Commentatio de vera materia sanguini purpureum colorem impertientis natura
3275:
3241:
3097:
3020:
2078:
Hemoglobin concentration measurement is among the most commonly performed
8803:
8563:
8476:
7889:
7765:
7363:
7313:
5641:
4115:
4086:
2916:
2912:
2697:
2676:
2537:
2509:
2470:
2408:
2163:
2103:
1967:
1875:
1537:
development. They may also be pathologic mutant forms of hemoglobin in a
1435:
1423:
1363:
1351:
1288:
In similar fashion, hemoglobin also has competitive binding affinity for
1262:
1019:
810:
806:
784:
741:
690:
678:
660:
646:
612:
close together on chromosome 16, while the beta subunit is coded by gene
564:
380:
97:
7210:
Can't Live Without It: The story of hemoglobin in sickness and in health
3070:
Dominguez de Villota ED, Ruiz Carmona MT, Rubio JJ, de Andrés S (1981).
2473:, which is unable to reduce nitrogen gas in the presence of free oxygen.
1716:
9000:
8880:
8618:
8597:
8594:
8523:
8481:
7827:
7641:
7418:
7413:
6895:"Hemoglobin is Expressed by Mesangial Cells and Reduces Oxidant Stress"
6678:
5461:
4680:"Hemoglobin based oxygen carriers: how much methemoglobin is too much?"
3913:"Hemoglobin Is Expressed by Mesangial Cells and Reduces Oxidant Stress"
2545:
2478:
2441:
2397:
2312:
2137:
2079:
1538:
1047:
879:
857:
568:
481:
465:
434:
368:
314:
279:
255:
6592:
6335:
Philosophical Transactions of the Royal Society B: Biological Sciences
6168:
Handin, Robert I.; Lux, Samuel E. and StosselBlood, Thomas P. (2003).
4557:"A brief history of hemoglobins: plant, animal, protist, and bacteria"
4437:
3038:
2991:
2536:
Outside the brain, hemoglobin has non-oxygen-carrying functions as an
2117:
Women: 12.1 to 15.1 g/dL (121 to 151 g/L, or 7.51 to 9.37 mmol/L)
1673:
1640:
1589:
356:
group in the globin protein, releasing it at the same time as oxygen.
91:
8464:
7703:
5102:
4259:
3879:
3805:
2727:– iridium organometallic complex notable for its ability to bind to O
2599:
2584:
2501:
2455:
2386:
2267:
2222:, which consists of a small sensing device that clips to the finger.
2120:
Children: 11 to 16 g/dL (110 to 160 g/L, or 6.83 to 9.93 mmol/L)
2114:
Men: 13.8 to 18.0 g/dL (138 to 180 g/L, or 8.56 to 11.17 mmol/L)
2099:
1979:
1948:
1899:
1863:
1550:
1465:
metabolic processes when oxygen is present at low partial pressures.
1197:
1161:
1157:
1149:
1145:
1120:
A schematic visual model of oxygen-binding process, showing all four
871:
849:
845:
829:
814:
493:
442:
6285:
5509:
5495:(12th ed.). Philadelphia, Pa.: Saunders/Elsevier. p. 502.
1898:. Hemoglobin deficiency is, in general, strictly distinguished from
1855:
is then cleared from the circulation via the hemoglobin transporter
81:
subunits are in red and blue, respectively, and the iron-containing
6624:
5925:
William, C. Wilson; Grande, Christopher M.; Hoyt, David B. (2007).
5516:
Rhodes, Carl E.; Denault, Deanna; Varacallo, Matthew (2019-03-04).
5279:
Zimmer EA, Martin SL, Beverley SM, Kan YW, Wilson AC (1980-04-01).
5137:
Storz, Jay F.; Opazo, Juan C.; Hoffmann, Federico G. (2013-02-01).
4737:
3257:"Hemoglobin Expression in Nonerythroid Cells: Novel or Ubiquitous?"
3119:
Rhodes, Carl E.; Denault, Deanna; Varacallo, Matthew (2019-03-04).
2632:
2435:
2308:
2304:
2235:
2231:
1952:
1871:
1504:
1278:
1055:
979:. It does not, however, help to counteract a decrease in blood pH.
841:
791:
729:
620:
441:
for his work determining the molecular structure of hemoglobin and
303:
120:
61:
7342:
6652:
5747:
700:
also promote efficient use of oxygen at low partial pressures of O
8946:
7881:
6625:"Cercacor – How Ember's non-invasive hemoglobin technology works"
5841:(7th ed.). Hoboken, NJ: John Wiley & Sons. p. 797.
4623:
School of Chemistry – Bristol University – UK. Web. 12 Oct. 2009.
2428:
2320:
1991:
1649:
1312:
1297:
1289:
1129:
1121:
1108:
have lost their hemoglobin genes as an adaptation to cold water.
1086:
1003:
867:
837:
833:
721:
674:
665:
239:
2262:
but not one that deals with oxygen transport (for example, many
7898:
7408:
6711:
Zal F, Lallier FH, Green BN, Vinogradov SN, Toulmond A (1996).
6118:"Hemoglobin: Emerging marker in stable coronary artery disease"
3725:
Hoppe-Seyler F (1866). "Über die oxydation in lebendem blute".
3700:. National Aeronautics and Space Administration. Archived from
2712:
2263:
2255:
2247:
2243:
1887:
1867:
1557:
1403:
1367:
1316:
1282:
1240:
can also be transported by hemoglobin; it is bound to specific
1133:
725:
654:
604:. Alpha 1 and alpha 2 subunits are respectively coded by genes
560:
531:
411:
400:
310:
258:
contain hemoglobin, with the sole exception of the fish family
247:
130:
78:
7332:
New hemoglobin type causes mock diagnosis with pulse oxymeters
6006:
5906:
Biology-Online.org --> Dictionary » H » Hypoxemia
2777:
1410:
Hence, blood with high carbon dioxide levels is also lower in
480:, it became possible to sequence protein structures. In 1959,
348:. The molecule also carries the important regulatory molecule
7950:
7880:
7354:
5580:(11 ed.). Philadelphia: Elsevier Saunders. p. 511.
2316:
2300:
2296:
2239:
2095:
1995:
1856:
1500:
1452:
In people acclimated to high altitudes, the concentration of
1241:
499:
The role of hemoglobin in the blood was elucidated by French
430:
353:
263:
6945:
Pharmacy Practice Manual: A Guide to the Clinical Experience
6525:
4936:
Essentials of Oxygenation: Implication for Clinical Practice
3782:
8059:
8047:
8042:
7974:
7885:
7805:
7504:
5780:. American Association for Clinical Chemistry. 2007-11-10.
3504:"Engelhard & Rose on the Colouring Matter of the Blood"
2822:
2816:
2795:
2783:
2580:
2212:
2091:
1962:
Some mutations in the globin chain are associated with the
1924:. However, it can also be pathologically altered in, e.g.,
1415:
1141:
1137:
1125:
802:
772:
749:
594:
588:
576:
544:
525:
519:
271:
267:
243:
185:
167:
141:
82:
7225:
7003:
4473:
Van Kessel, Hans (2002). "Proteins – Natural Polyamides".
4421:"Characteristics of RNA degradation in the erythroid cell"
2166:
concentration can be measured by the concentration of Hb A
1874:
in tissues and transported in plasma by beta globulins as
689:) have caused the protein to have less of an affinity for
586:(the main form of hemoglobin in adults) is coded by genes
418:, in which hemoglobin leaks from red blood cells into the
359:
Hemoglobin is also found in other cells, including in the
8289:
8030:
6710:
5348:"A signature of the T → R transition in human hemoglobin"
2975:
2801:
2789:
2687:
1311:
The iron atom in the heme group must initially be in the
1058:, the blue to purplish color that tissues develop during
983:, or breathing, may reverse this condition by removal of
821:
768:
600:
203:
5346:
Mihailescu, Mihaela-Rita; Russu, Irina M. (2001-03-27).
5204:
4779:
4777:
4326:
3254:
2225:
1677:) – The most common with a normal amount over 95%
1249:
nitric oxide to tissues in which oxygen levels are low.
1054:. This difference also accounts for the presentation of
7139:
6328:
5748:
Rang, H.P.; Dale M.M.; Ritter J.M.; Moore P.K. (2003).
5645:
AJP: Regulatory, Integrative and Comparative Physiology
5278:
4677:
4507:
University of Massachusetts Amherst. Web. 23 Oct. 2009.
4412:
3021:
Weed, Robert I.; Reed, Claude F.; Berg, George (1963).
1951:(accelerated breakdown of red blood cells), associated
1411:
1319:(Fe) state without oxygen converts hemoglobin into "hem
1203:
6892:
6854:"Hemoglobin Is Expressed by Alveolar Epithelial Cells"
5515:
3910:
3118:
2086:. For example, it is typically tested before or after
890:
In adult humans, the most common hemoglobin type is a
683:
Oreotrochilus, A. castelnaudii, C. violifer, P. gigas,
313:, hemoglobin makes up about 96% of a red blood cell's
7326:
6491:
Rolfe, P. (2000). "Invivonear-Infraredspectroscopy".
5801:
4774:
3749:"Structural biology: How proteins got their close-up"
3454:"Max Perutz, Father of Molecular Biology, Dies at 87"
3317:
Biagioli M, Pinto M, Cesselli D, et al. (2009).
3316:
3161:. Hagerstwon, MD: Lippincott Williams & Wilkins.
2825:
2804:
2771:
2323:
may contain both globin and other types of proteins.
1990:
To a small extent, hemoglobin A slowly combines with
1862:
The other major final product of heme degradation is
1553:, and are thus considered non-pathological variants.
1472:
affinity under unfavorable conditions. Fish use both
1140:
atoms, it binds to the iron (red sphere) in the flat
1080:
7358:
7049:
6243:. 4th ed., p. 919. Philadelphia: Saunders Elsevier.
5839:
Textbook of Biochemistry: With Clinical Correlations
5712:
2798:
2792:
2628:
2350:
from the water to produce energy to make food from H
1977:
There is a group of genetic disorders, known as the
1842:
1821:
with one adult gene and one sickle cell disease gene
6851:
5804:
Biochemical and Biophysical Research Communications
5080:
2952:. Englewood Cliffs, New Jersey, US: Prentice Hall.
2819:
2813:
2810:
2786:
2780:
2774:
1947:(smaller than normal). Other anemias are rarer. In
582:There is more than one hemoglobin gene. In humans,
7004:Moran L, Horton RA, Scrimgeour G, Perry M (2011).
5621:(Eighth ed.). New York: W. H. Freeman. 2015.
5575:
5136:
3154:
1545:, are responsible for diseases and are considered
1445:in lungs), and efficient in unloading (unloading O
375:, lungs, retinal pigment epithelium, hepatocytes,
5018:
4958:
4678:Linberg R, Conover CD, Shum KL, Shorr RG (1998).
4510:
4221:Reed, Leslie. "Adaptation found in mouse genes."
3383:National Heart, Lung, and Blood Institute (NHLBI)
2487:
2013:whose glucose usually runs high, the percent Hb A
1987:was probably the most famous porphyria sufferer.
1881:
1160:ring (see moving diagram). At the same time, the
1136:is not shown in this model, but, for each of the
1022:, whereas both oxygen and high-spin iron(II) are
805:group. Each protein chain arranges into a set of
748:is lost in mammalian red blood cells, but not in
9035:
7031:"Take a sneak peek at the MUHC's art collection"
6329:Ferrari, M.; Binzoni, T.; Quaresima, V. (1997).
4728:. Worthington-biochem.com. Retrieved 2013-09-05.
3966:
3964:
2374:
1906:of oxygen in blood, although both are causes of
1521:
7355:Animation of hemoglobin: from deoxy to oxy form
6653:L. Int Panis; B. Goddeeris; R Verheyen (1995).
6115:
6053:
5894:hypoxemia (reduced oxygen tension in the blood)
5522:. Treasure Island (FL): StatPearls Publishing.
5345:
5208:"Origin of complexity in haemoglobin evolution"
5076:
5074:
5014:
5012:
4933:
4876:, 3rd. ed., Fig. 07_06, John Wiley & Sons.
4840:
4548:
4266:Proceedings of the National Academy of Sciences
3409:
3125:. Treasure Island (FL): StatPearls Publishing.
2178:of hemoglobin A with glucose. A higher glucose
399:systems such as the nitrogen-fixing nodules of
8978:aPTT-based activated protein C resistance test
6852:Newton DA, Rao KM, Dluhy RA, Baatz JE (2006).
6792:
6428:
6262:"Hematocrit (HCT) or Packed Cell Volume (PCV)"
6170:Blood: Principles & Practice of Hematology
5927:"Pathophysiology of acute respiratory failure"
5558:, 3rd ed. New York: Worth Publishers. p. 217,
5493:Guyton and Hall textbook of medical physiology
5200:
5198:
4938:. Jones & Bartlett Learning. p. 194.
4468:
4466:
3861:
3835:Perutz MF (1960). "Structure of haemoglobin".
3724:
1193:curve associated with noncooperative binding.
1073:. In contrast, oxygenated hemoglobin exhibits
894:(which contains four subunit proteins) called
8983:ETP-based activated protein C resistance test
8579:
7866:
7379:
6969:Holden, Constance (2005). "Blood and Steel".
6899:Journal of the American Society of Nephrology
6056:Acta Obstetricia et Gynecologica Scandinavica
5132:
5130:
5128:
4651:
3961:
3917:Journal of the American Society of Nephrology
3645:Der Chemismus in der thierischen Organisation
3405:
3403:
2925:(18th ed.). Cambridge University Press.
2559:
7022:
6385:
5071:
5009:
4849:"The Medical Biochemistry Page – Hemoglobin"
4684:Artif Cells Blood Substit Immobil Biotechnol
3828:
3718:
2971:
2969:
2258:. Or, they may have a recognizable separate
1817:Hemoglobin AS – A heterozygous form causing
1507:is able to take oxygen from maternal blood.
1034:) or in a covalent charge-transfer complex.
998:(R). Various factors such as low pH, high CO
809:structural segments connected together in a
266:carries oxygen from the respiratory organs (
7261:Cold Spring Harbor Perspectives in Medicine
6795:"Hemoglobin induction in mouse macrophages"
5406:
5195:
4846:
4463:
4186:. Labtestsonline.org. Retrieved 2013-09-05.
4146:
4142:
4140:
3977:Cold Spring Harbor Perspectives in Medicine
3855:
3742:
3740:
3691:"A NASA Recipe For Protein Crystallography"
3312:
3310:
3308:
3306:
3304:
3219:
3213:
2303:often have single-globin hemoglobins. Many
1358:, carbon dioxide reacts with water to give
8593:
8586:
8572:
7873:
7859:
7393:
7386:
7372:
7191:Force of Nature: The Life of Linus Pauling
6751:
6148:Society for Biomedical Diabetes Research.
5964:
5671:
5125:
4523:. Cambridge University Press. p. 95.
4472:
3776:
3671:Funke O (1851). "Über das milzvenenblut".
3400:
1181:the oxygen binding curve of hemoglobin is
1077:, a weak repulsion from a magnetic field.
1037:
641:, which was the first human disease whose
623:in the genes for hemoglobin can result in
60:
8639:Mean corpuscular hemoglobin concentration
8554:disorders of globin and globulin proteins
7288:
6918:
6869:
6828:
6818:
6769:
6728:
6600:
6543:
6362:
6133:
5982:
5389:
5371:
5322:
5304:
5247:
5178:
5054:
5044:
4992:
4910:
4695:
4590:
4580:
4516:
4446:
4436:
4370:
4352:
4303:
4285:
4149:"A Syllabus of Human Hemoglobin Variants"
4004:
3944:
3887:
3834:
3760:
3568:
3519:
3496:
3474:
3468:
3354:
3344:
3284:
3274:
3087:
3046:
2966:
1943:(lacking the red hemoglobin pigment) and
1910:(insufficient oxygen supply to tissues).
836:molecules cyclically linked together (by
575:from a segment of DNA, the corresponding
7254:
7118:
6239:Murray S.S. & McKinney E.S. (2006).
6035:"Definition of Glycosylated Hemoglobin."
5958:
5576:Guyton, Arthur C.; John E. Hall (2006).
4554:
4137:
3970:
3746:
3737:
3641:
3301:
2922:Cambridge English Pronouncing Dictionary
2563:
2291:showing red hemoglobin-containing plumes
2280:
2213:Athletic tracking and self-tracking uses
2186:. Because the reaction is slow, the Hb A
2065:
1715:
1397:
1115:
767:
659:
429:
8968:Ristocetin-induced platelet aggregation
8930:Activated protein C–protein C inhibitor
7257:"Evolution of Hemoglobin and Its Genes"
6493:Annual Review of Biomedical Engineering
6241:Foundations of Maternal-Newborn Nursing
5412:
4892:
4886:
4815:
3973:"Evolution of hemoglobin and its genes"
3670:
3648:(in German). Leipzig: F. A. Brockhaus.
3612:
2246:. Since many of these proteins contain
1732:Abnormal forms that occur in diseases:
832:. This porphyrin ring consists of four
724:of immature red blood cells, while the
14:
9036:
7168:
6968:
6659:Netherlands Journal of Aquatic Ecology
6455:
5918:
5836:
5635:
5447:
5441:
5019:Bren KL, Eisenberg R, Gray HB (2015).
4812:Biology @ Davidson. Web. 12 Oct. 2009.
4633:WikiPremed > Coordination Chemistry
4401:from the original on December 26, 2007
4027:
3620:. Bulgin and Rosser. Part 1, p. 9–13.
3508:Edinburgh Medical and Surgical Journal
3248:
3181:
3148:
2613:Montreal artist Nicolas Baier created
820:A heme group consists of an iron (Fe)
8567:
7854:
7367:
7187:
7067:from the original on February 1, 2016
7037:from the original on February 5, 2016
7028:
6948:. Lippincott Williams & Wilkins.
6490:
6172:. Lippincott Williams & Wilkins,
5933:. Taylor & Francis. p. 430.
5706:
5602:Lecture – 12 Myoglobin and Hemoglobin
5143:Molecular Phylogenetics and Evolution
4425:The Journal of Clinical Investigation
4418:
4198:"Hemoglobinopathies and Thalassemias"
3664:
3583:
3542:
3262:International Journal of Inflammation
2903:
2875:
2226:Analogues in non-vertebrate organisms
2199:functional magnetic resonance imaging
1652:(newborns inmmediately after birth):
1549:. Other variants cause no detectable
637:. The best known hemoglobinopathy is
492:, who sequenced the globular protein
403:plants, preventing oxygen poisoning.
27:Metalloprotein that binds with oxygen
9011:Nitro blue tetrazolium chloride test
7752:oxygen–hemoglobin dissociation curve
7008:. Boston, MA: Pearson. p. 127.
5556:Lehninger Principles of Biochemistry
5490:
3862:de Chadarevian, Soraya (June 2018).
3747:Stoddart, Charlotte (1 March 2022).
3475:Engelhart, Johann Friedrich (1825).
1922:oxygen–hemoglobin dissociation curve
1341:Oxygen-hemoglobin dissociation curve
1204:Binding of ligands other than oxygen
943:
790:In most vertebrates, the hemoglobin
763:
668:'s alignment tool available online.
395:serves to scavenge oxygen away from
325:per gram, which increases the total
8973:Activated protein C resistance test
6941:
6431:Exercise and Sport Sciences Reviews
5727:10.1146/annurev.ph.50.030188.001113
3642:Hünefeld, Friedrich Ludwig (1840).
2979:The Journal of Experimental Biology
425:
24:
7678:hypoxic pulmonary vasoconstriction
7083:
6793:Liu L, Zeng M, Stamler JS (1999).
6116:Padmanaban, P.; Toora, B. (2011).
5554:Nelson, D. L.; Cox, M. M. (2000).
4934:Ahrens; Kimberley, Basham (1993).
4236:"Mammoths had 'anti-freeze' blood"
4195:
3652:from the original on 14 April 2021
2454:Found in many annelids, including
2055:
2029:. This elevation may be caused by
1966:, such as sickle-cell disease and
1189:-shaped, as opposed to the normal
1081:Evolution of vertebrate hemoglobin
990:Hemoglobin exists in two forms, a
866:The iron ion may be either in the
246:that facilitates the transport of
25:
9070:
8864:Dilute Russell's viper venom time
8649:Red blood cell distribution width
7306:
4477:. Toronto: Thomson. p. 122.
4155:. Pennsylvania State University.
3481:(in Latin). Göttingen: Dietrich.
2440:, they are found in the blood of
1843:Degradation in vertebrate animals
1747:) – A variant form of hemoglobin.
987:, thus causing a shift up in pH.
728:protein parts are synthesized by
567:, long folded chains of specific
8876:Calibrated automated thrombogram
6997:
6962:
6935:
6886:
6845:
6786:
6771:10.1111/j.1432-1033.2004.04248.x
6745:
6704:
6646:
6617:
6568:
6519:
6484:
6449:
6422:
6379:
6331:"Oxidative metabolism in muscle"
6322:
6279:
6044:Medicine Net. Web. 12 Oct. 2009.
5984:10.1097/00152193-199626050-00013
5931:Trauma, Volume II: Critical Care
4912:10.1016/j.pbiomolbio.2005.04.001
3971:Hardison, Ross C. (2012-12-01).
3543:Adair, Gilbert Smithson (1925).
2881:Longman Pronunciation Dictionary
2844:
2767:
2645:
2631:
1985:George III of the United Kingdom
1111:
951:
535:, reflecting the fact that each
290:grams of hemoglobin in every 100
6858:Journal of Biological Chemistry
6693:from the original on 2018-09-05
6635:from the original on 2016-11-04
6545:10.1152/japplphysiol.00185.2017
6268:from the original on 2008-01-02
6254:
6233:
6219:"haemoglobin (reference range)"
6211:
6182:
6162:
6142:
6109:
6090:
6047:
6028:
6017:from the original on 2015-10-15
5999:
5947:from the original on 2016-11-17
5899:
5872:
5855:
5830:
5795:
5784:from the original on 2008-09-20
5766:
5741:
5611:
5594:
5569:
5548:
5534:from the original on 2021-08-27
5484:
5450:Journal of Experimental Biology
5339:
5272:
4952:
4927:
4866:
4855:from the original on 2012-03-04
4796:
4793:MedicineNet. Web. 12 Oct. 2009.
4712:
4671:
4660:from the original on 2021-07-18
4645:
4626:
4607:
4537:from the original on 2016-11-17
4491:
4387:
4320:
4253:
4242:from the original on 2010-05-04
4228:
4215:
4189:
4170:
4159:from the original on 2008-12-11
4126:from the original on 2020-08-01
4108:
4097:from the original on 2020-08-01
4079:
4068:from the original on 2019-12-26
4021:
3904:
3683:
3635:
3624:from the original on 2022-01-31
3606:
3595:from the original on 2022-01-31
3577:
3536:
3485:from the original on 2020-06-16
3446:
3389:from the original on 2019-04-09
3222:New England Journal of Medicine
3202:from the original on 2016-04-26
3182:Patton, Kevin T. (2015-02-10).
3175:
3137:from the original on 2021-08-27
2835:
2705:(ferric Hb, or ferrihemoglobin)
2619:McGill University Health Centre
2274:, sulfide compounds, and even O
1838:to produce sickle cell disease.
469:described a few years later by
336:(about 20–25% of the total) as
66:Structure of human hemoglobin.
8905:Coagulation activation markers
8778:Erythrocyte sedimentation rate
7323:National Anemia Action Council
7029:Henry, Sean (August 7, 2014).
6983:10.1126/science.309.5744.2160d
6505:10.1146/annurev.bioeng.2.1.715
6122:Chronicles of Young Scientists
5915:last modified 29 December 2008
5578:Textbook of Medical Physiology
4825:. altitude.org. Archived from
3837:Brookhaven Symposia in Biology
3112:
3063:
3014:
2939:
2897:
2869:
2747:
2488:Presence in nonerythroid cells
1896:blood oxygen-carrying capacity
1882:Diseases related to hemoglobin
1499:), is found in the developing
1273:, which may cause the skin of
1252:
13:
1:
8915:Thrombin–antithrombin complex
8663:White blood cell differential
6532:Journal of Applied Physiology
6400:10.1016/S0301-0082(98)00093-8
6150:SI Unit Conversion Calculator
4985:10.1016/S0006-3495(93)81441-3
4823:"Hemoglobin saturation graph"
3424:10.1152/physrev.2001.81.2.569
2735:
2375:Other oxygen-binding proteins
2074:Boston Blood Donation Center.
1522:Types of hemoglobin in humans
1487:A variant hemoglobin, called
1438:. This is seen in bony fish.
1334:
653:. All these diseases produce
294:mL of blood. Hemoglobin is a
149:
8900:Overall hemostatic potential
7171:Review of Medical Physiology
7125:(third ed.). Harcourt.
7109:Resources in other libraries
6300:10.1097/CCM.0b013e3182227e2d
6196:. 2013-08-16. Archived from
5867:Dorland's Medical Dictionary
5692:10.1016/0022-2836(84)90249-3
5680:Journal of Molecular Biology
5541:– via NCBI Bookshelf.
5519:Physiology, Oxygen Transport
5427:10.1016/0968-0004(89)90026-1
4874:Fundamentals of Biochemistry
4034:The American Biology Teacher
4028:Offner, Susan (2010-04-01).
3460:. 2002-02-08. Archived from
3188:. Elsevier Health Sciences.
3122:Physiology, Oxygen Transport
1104:Most ice fish of the family
1069:; it is weakly attracted to
874:state, but ferrihemoglobin (
711:
517:) is derived from the words
7:
8822:Partial thromboplastin time
8788:Monocyte distribution width
8634:Mean corpuscular hemoglobin
7710:Ventilation/perfusion ratio
7561:pulmonary stretch receptors
7273:10.1101/cshperspect.a011627
7057:"Lustre (Hémoglobine) 2014"
6470:10.1016/j.ymeth.2008.04.005
5750:Pharmacology, Fifth Edition
5715:Annual Review of Physiology
5163:10.1016/j.ympev.2012.07.013
4752:10.1152/jappl.2001.90.2.511
3989:10.1101/cshperspect.a011627
3234:10.1056/NEJM199801223380407
3155:Costanzo, Linda S. (2007).
3144:– via NCBI Bookshelf.
2624:
2604:Heart of Steel (Hemoglobin)
2569:Heart of Steel (Hemoglobin)
1065:Deoxygenated hemoglobin is
928:are bound to each other by
550:
10:
9075:
8761:Hemoglobin electrophoresis
7742:alveolar–arterial gradient
7255:Hardison, Ross C. (2012).
7006:Principles of Biochemistry
5965:McGaffigan, P. A. (1996).
5816:10.1016/j.bbrc.2005.08.020
5657:10.1152/ajpregu.00536.2006
2862:
2753:from the Greek word αἷμα,
2560:In history, art, and music
2378:
2090:. Results are reported in
2059:
1338:
1224:such as carbon dioxide (CO
278:which powers the animal's
8993:
8910:Prothrombin fragments 1+2
8871:Thrombin generation assay
8802:
8702:
8668:Absolute neutrophil count
8604:
8549:
8516:
8490:
8455:
8448:
8423:
8402:
8367:
8260:
8200:
8161:
8094:
8083:
8074:
7997:
7922:
7915:
7906:
7897:
7815:
7691:
7665:
7623:respiratory minute volume
7576:
7535:ventral respiratory group
7494:
7401:
7240:10.1016/j.jmb.2005.11.006
7154:10.1016/j.ahj.2005.10.008
7104:Resources in your library
6752:Minic Z, Hervé G (2004).
6223:General Practice Notebook
6068:10.3109/00016348409155523
5232:10.1038/s41586-020-2292-y
4697:10.3109/10731199809119772
3762:10.1146/knowable-022822-1
2883:(3rd ed.). Longman.
1926:carbon monoxide poisoning
1607:Hemoglobin Portland II (ζ
1529:are a part of the normal
1430:-saturation curve to the
1267:carbon monoxide detectors
977:oxidative phosphorylation
961:physiological respiration
439:Nobel Prize for chemistry
148:
137:
126:
108:
59:
39:
34:
7530:dorsal respiratory group
7424:obligate nasal breathing
7208:Hazelwood, Loren (2001)
7173:(21st ed.). Lange.
6388:Progress in Neurobiology
5025:Proc Natl Acad Sci U S A
4642:. Retrieved July 2, 2009
4046:10.1525/abt.2010.72.4.10
2949:Human Biology and Health
2740:
2529:), but rather is due to
2366:for the bacteria, and CO
2153:brain–computer interface
2031:congenital heart disease
1596:Hemoglobin Portland I (ζ
1510:Hemoglobin also carries
1362:, which decomposes into
1329:nitric oxide dioxygenase
854:coordinate covalent bond
486:Nobel Prize in Chemistry
476:With the development of
282:. A healthy human has 12
8832:Activated clotting time
8644:Mean corpuscular volume
7732:pulmonary gas pressures
7343:www.life-of-science.net
7214:Nova Science Publishers
6820:10.1073/pnas.96.12.6643
6730:10.1074/jbc.271.15.8875
6629:technology.cercacor.com
6190:"Hemoglobin Level Test"
6135:10.4103/2229-5186.82971
5890:Encyclopædia Britannica
5046:10.1073/pnas.1515704112
4582:10.1073/pnas.93.12.5675
4354:10.1073/pnas.0405949101
4287:10.1073/pnas.1315456110
4225:, 11 Aug. 2009: EBSCO.
3346:10.1073/pnas.0813216106
2673:(Hb associated with CO)
2082:, usually as part of a
1902:, defined as decreased
1726:Br. Med. Bull. 32, 282.
1454:2,3-Bisphosphoglycerate
1038:Deoxygenated hemoglobin
885:methemoglobin reductase
794:is an assembly of four
555:Hemoglobin consists of
416:intravascular hemolysis
361:A9 dopaminergic neurons
9059:Respiratory physiology
9044:Protein heteropolymers
8766:Sickle solubility test
8658:White blood cell count
8629:Red blood cell indices
7486:mechanical ventilation
7395:Respiratory physiology
7194:. Simon and Schuster.
6911:10.1681/ASN.2007101085
6871:10.1074/jbc.M509314200
6355:10.1098/rstb.1997.0049
6288:Critical Care Medicine
5491:Hall, John E. (2010).
5373:10.1073/pnas.071493598
5306:10.1073/pnas.77.4.2158
4652:Basic Biology (2015).
4561:Proc Natl Acad Sci USA
4517:Steinberg, MH (2001).
4498:"Hemoglobin Tutorial."
4419:Burka, Edward (1969).
4395:"Hemoglobin Synthesis"
3929:10.1681/ASN.2007101085
3727:Med-chem Untersuch Lab
3570:10.1098/rspa.1925.0126
3185:Anatomy and Physiology
3089:10.1093/bja/53.12.1325
2663:(Hb associated with CO
2576:
2346:S from the vent with O
2292:
2174:is the product of the
2075:
1937:iron deficiency anemia
1729:
1407:
1214:competitive inhibitors
1153:
917:In human infants, the
776:
691:inositol hexaphosphate
669:
625:variants of hemoglobin
563:molecules), which are
459:Gilbert Smithson Adair
445:
406:The medical condition
85:groups in green. From
9054:Equilibrium chemistry
8963:Von Willebrand factor
8942:Euglobulin lysis time
8881:ST Genesia-based test
7737:alveolar gas equation
7673:pulmonary circulation
7119:Campbell, MK (1999).
6264:. DoctorsLounge.com.
6007:"NGSP: HbA1c and eAG"
5977:(5): 41–46, quiz 46.
5774:"Hemoglobin Variants"
4899:Prog Biophys Mol Biol
4555:Hardison, RC (1996).
2567:
2284:
2176:irreversible reaction
2162:Long-term control of
2069:
1920:, causing an altered
1719:
1700:(fetal hemoglobin) (α
1659:(adult hemoglobin) (α
1401:
1354:. Through the enzyme
1339:Further information:
1331:function of globins.
1119:
965:pulmonary capillaries
771:
744:. At this point, the
663:
478:X-ray crystallography
433:
327:blood oxygen capacity
8956:-antiplasmin complex
8893:Thrombodynamics test
8859:Ecarin clotting time
8748:Kleihauer–Betke test
8680:Mean platelet volume
8624:Red blood cell count
8606:Complete blood count
7792:respiratory quotient
7647:body plethysmography
7566:Hering–Breuer reflex
7441:pulmonary surfactant
4147:Huisman THJ (1996).
3613:Beddoes, T. (1796).
3514:(90): 95–102. 1827.
2715:, colored blood-red)
2683:Complete blood count
2615:Lustre (Hémoglobine)
2512:, and in all mature
2285:The giant tube worm
2182:results in more Hb A
2084:complete blood count
1832:Hemoglobin Hopkins-2
1200:has been discussed.
781:quaternary structure
262:. Hemoglobin in the
8888:Thromboelastography
8410:Glycated hemoglobin
8380:Carbaminohemoglobin
7635:Lung function tests
7469:hyperresponsiveness
7169:Ganong, WF (2003).
7061:Art Public Montréal
6942:Boh, Larry (2001).
6811:1999PNAS...96.6643L
6671:1995NJAqE..29....1P
6347:1997RSPTB.352..677F
6194:Ibdcrohns.about.com
5415:Trends Biochem. Sci
5364:2001PNAS...98.3773M
5297:1980PNAS...77.2158Z
5224:2020Natur.581..480P
5155:2013MolPE..66..469S
5095:1975Natur.253..603G
5037:2015PNAS..11213123B
4977:1993BpJ....64..803O
4965:Biophysical Journal
4573:1996PNAS...93.5675H
4475:Nelson Chemistry 12
4345:2004PNAS..10114300B
4278:2013PNAS..11020669P
4238:. BBC. 2010-05-02.
4177:Hemoglobin Variants
3798:1960Natur.185..416P
3561:1925RSPSA.109..292A
3337:2009PNAS..10615454B
3276:10.1155/2014/803237
2986:(Pt 10): 1791–802.
2661:Carbaminohemoglobin
2596:Julian Voss-Andreae
2573:Julian Voss-Andreae
2540:and a regulator of
2523:Parkinson's disease
2381:Respiratory pigment
2003:glycated hemoglobin
1972:hemoglobin variants
1527:Hemoglobin variants
1420:carbaminohemoglobin
1234:carbaminohemoglobin
1208:Besides the oxygen
1174:cooperative process
639:sickle-cell disease
629:hereditary diseases
539:of hemoglobin is a
338:carbaminohemoglobin
276:aerobic respiration
8718:Total blood volume
8692:Reticulocyte index
8687:Reticulocyte count
7802:diffusion capacity
7797:arterial blood gas
7777:carbonic anhydrase
7511:pneumotaxic center
7348:2017-03-07 at the
7337:2016-03-09 at the
7148:(1): 91.e1–91.e6.
6679:10.1007/BF02061785
6155:2013-03-09 at the
6102:2016-06-10 at the
6040:2014-01-23 at the
5911:2009-11-21 at the
5884:2009-02-02 at the
5862:"hemoglobinopathy"
5462:10.1242/jeb.023697
5456:(Pt 21): 3387–93.
4893:Shikama K (2006).
4808:2009-12-01 at the
4803:"Hemoglobin Home."
4789:2012-01-24 at the
4724:2017-03-15 at the
4638:2009-08-23 at the
4619:2009-11-13 at the
4503:2009-11-26 at the
4397:. April 14, 2002.
4223:Omaha World-Herald
4182:2006-11-05 at the
4153:Globin Gene Server
3584:Parry, CH (1794).
3549:Proc. R. Soc. Lond
3458:The New York Times
2719:Tegillarca granosa
2577:
2392:than transport it.
2293:
2260:circulatory system
2076:
2072:American Red Cross
2039:pulmonary fibrosis
1964:hemoglobinopathies
1935:and its resultant
1892:Hemoglobinopathies
1730:
1547:hemoglobinopathies
1543:sickle-cell anemia
1408:
1356:carbonic anhydrase
1222:allosteric ligands
1154:
1044:absorption spectra
975:by the process of
938:hydrophobic effect
926:polypeptide chains
777:
670:
634:hemoglobinopathies
471:Felix Hoppe-Seyler
446:
159:Chromosomal locus
40:(heterotetramer, (
9031:
9030:
9021:Immunophenotyping
8794:Osmotic fragility
8561:
8560:
8512:
8511:
8508:
8507:
8444:
8443:
8375:Carboxyhemoglobin
8363:
8362:
8256:
8255:
8070:
8069:
7848:
7847:
7756:Oxygen saturation
7722:zones of the lung
7461:airway resistance
7201:978-0-684-80909-0
7188:Hager, T (1995).
7180:978-0-07-140236-1
7132:978-0-03-024426-1
7090:Library resources
7015:978-0-321-70733-8
6955:978-0-7817-2541-5
6593:10.1002/hbm.10026
5940:978-1-4200-1684-0
5848:978-0-470-28173-4
5759:978-0-443-07202-4
5628:978-1-4641-2610-9
5587:978-0-7216-0240-0
5502:978-1-4160-4574-8
4945:978-0-86720-332-5
4847:King, Michael W.
4530:978-0-521-63266-9
4484:978-0-17-625986-0
4438:10.1172/jci106092
3753:Knowable Magazine
3698:Educational Brief
3195:978-0-323-31687-3
3168:978-0-7817-7311-9
3039:10.1172/JCI104747
2992:10.1242/jeb.02091
2959:978-0-13-981176-0
2932:978-0-521-15255-6
2890:978-1-4058-8118-0
2761:'ball, sphere' +
2671:Carboxyhemoglobin
2332:Riftia pachyptila
2288:Riftia pachyptila
2047:polycythemia vera
1819:sickle cell trait
1271:carboxyhemoglobin
1091:jawed vertebrates
992:taut (tense) form
959:is formed during
944:Oxygen saturation
828:ring, known as a
779:Hemoglobin has a
764:Structure of heme
698:circulatory lungs
543:with an embedded
221:
220:
217:
216:
16:(Redirected from
9066:
8920:Fibrinopeptide A
8817:Prothrombin time
8812:Clotting factors
8755:Hemoglobinopathy
8738:Fetal hemoglobin
8588:
8581:
8574:
8565:
8564:
8453:
8452:
8092:
8091:
8081:
8080:
7920:
7919:
7913:
7912:
7904:
7903:
7875:
7868:
7861:
7852:
7851:
7657:nitrogen washout
7516:apneustic center
7431:respiratory rate
7388:
7381:
7374:
7365:
7364:
7302:
7292:
7251:
7205:
7184:
7165:
7136:
7077:
7076:
7074:
7072:
7053:
7047:
7046:
7044:
7042:
7026:
7020:
7019:
7001:
6995:
6994:
6966:
6960:
6959:
6939:
6933:
6932:
6922:
6890:
6884:
6883:
6873:
6849:
6843:
6842:
6832:
6822:
6790:
6784:
6783:
6773:
6764:(15): 3093–102.
6749:
6743:
6742:
6732:
6708:
6702:
6701:
6699:
6698:
6650:
6644:
6643:
6641:
6640:
6621:
6615:
6614:
6604:
6572:
6566:
6565:
6547:
6523:
6517:
6516:
6488:
6482:
6481:
6453:
6447:
6446:
6426:
6420:
6419:
6383:
6377:
6376:
6366:
6341:(1354): 677–83.
6326:
6320:
6319:
6283:
6277:
6276:
6274:
6273:
6258:
6252:
6237:
6231:
6230:
6225:. Archived from
6215:
6209:
6208:
6206:
6205:
6186:
6180:
6166:
6160:
6146:
6140:
6139:
6137:
6113:
6107:
6094:
6088:
6087:
6051:
6045:
6032:
6026:
6025:
6023:
6022:
6003:
5997:
5996:
5986:
5962:
5956:
5955:
5953:
5952:
5922:
5916:
5903:
5897:
5876:
5870:
5859:
5853:
5852:
5834:
5828:
5827:
5799:
5793:
5792:
5790:
5789:
5778:Lab Tests Online
5770:
5764:
5763:
5745:
5739:
5738:
5710:
5704:
5703:
5675:
5669:
5668:
5639:
5633:
5632:
5615:
5609:
5603:
5598:
5592:
5591:
5573:
5567:
5552:
5546:
5545:
5540:
5539:
5513:
5507:
5506:
5488:
5482:
5481:
5445:
5439:
5438:
5410:
5404:
5403:
5393:
5375:
5343:
5337:
5336:
5326:
5308:
5276:
5270:
5269:
5251:
5218:(7809): 480–85.
5202:
5193:
5192:
5182:
5134:
5123:
5122:
5103:10.1038/253603a0
5089:(5493): 603–08.
5078:
5069:
5068:
5058:
5048:
5031:(43): 13123–27.
5016:
5007:
5006:
4996:
4956:
4950:
4949:
4931:
4925:
4924:
4914:
4890:
4884:
4872:Voet, D. (2008)
4870:
4864:
4863:
4861:
4860:
4844:
4838:
4837:
4835:
4834:
4819:
4813:
4800:
4794:
4781:
4772:
4771:
4735:
4729:
4716:
4710:
4709:
4699:
4675:
4669:
4668:
4666:
4665:
4649:
4643:
4630:
4624:
4611:
4605:
4604:
4594:
4584:
4552:
4546:
4545:
4543:
4542:
4514:
4508:
4495:
4489:
4488:
4470:
4461:
4460:
4450:
4440:
4416:
4410:
4409:
4407:
4406:
4391:
4385:
4384:
4374:
4356:
4339:(39): 14300–04.
4324:
4318:
4317:
4307:
4289:
4272:(51): 20669–74.
4257:
4251:
4250:
4248:
4247:
4232:
4226:
4219:
4213:
4212:
4210:
4209:
4200:. Archived from
4193:
4187:
4174:
4168:
4167:
4165:
4164:
4144:
4135:
4134:
4132:
4131:
4112:
4106:
4105:
4103:
4102:
4083:
4077:
4076:
4074:
4073:
4025:
4019:
4018:
4008:
3968:
3959:
3958:
3948:
3923:(8): 1500–1508.
3908:
3902:
3901:
3891:
3880:10.1002/pro.3417
3874:(6): 1136–1143.
3859:
3853:
3852:
3832:
3826:
3825:
3806:10.1038/185416a0
3792:(4711): 416–22.
3780:
3774:
3773:
3771:
3769:
3764:
3744:
3735:
3734:
3722:
3716:
3715:
3713:
3712:
3706:
3695:
3687:
3681:
3680:
3668:
3662:
3661:
3659:
3657:
3639:
3633:
3632:
3630:
3629:
3610:
3604:
3603:
3601:
3600:
3581:
3575:
3574:
3572:
3555:(750): 292–300.
3540:
3534:
3533:
3523:
3500:
3494:
3493:
3491:
3490:
3472:
3466:
3465:
3450:
3444:
3443:
3407:
3398:
3397:
3395:
3394:
3375:
3369:
3368:
3358:
3348:
3331:(36): 15454–59.
3314:
3299:
3298:
3288:
3278:
3252:
3246:
3245:
3217:
3211:
3210:
3208:
3207:
3179:
3173:
3172:
3152:
3146:
3145:
3143:
3142:
3116:
3110:
3109:
3091:
3067:
3061:
3060:
3050:
3018:
3012:
3011:
2973:
2964:
2963:
2943:
2937:
2936:
2901:
2895:
2894:
2873:
2856:
2848:
2842:
2839:
2833:
2832:
2831:
2828:
2827:
2824:
2821:
2818:
2815:
2812:
2807:
2806:
2803:
2800:
2797:
2794:
2791:
2788:
2785:
2782:
2779:
2776:
2773:
2757:'blood' + Latin
2751:
2693:Hemoglobinometer
2655:
2650:
2649:
2648:
2641:
2636:
2635:
2608:weathering steel
2514:oligodendrocytes
2498:substantia nigra
2062:Hemoglobinometer
1904:partial pressure
1798:hemolytic anemia
1762:Hemoglobin Barts
1710:beta-thalassemia
1676:
1643:
1592:
1489:fetal hemoglobin
1302:hydrogen sulfide
1028:superoxide anion
967:adjacent to the
919:fetal hemoglobin
912:molecular weight
796:globular protein
557:protein subunits
541:globular protein
426:Research history
383:, and regulates
365:substantia nigra
320:
293:
289:
285:
150:
94:
77:
71:
64:
50:
45:
32:
31:
21:
9074:
9073:
9069:
9068:
9067:
9065:
9064:
9063:
9034:
9033:
9032:
9027:
9006:Blood viscosity
8989:
8955:
8925:Fibrin monomers
8798:
8743:Apt–Downey test
8730:Red cell volume
8705:red blood cells
8703:Other tests of
8698:
8600:
8592:
8562:
8557:
8545:
8534:Cytochrome P450
8504:
8486:
8440:
8419:
8398:
8389:Deoxyhemoglobin
8359:
8355:
8351:
8341:
8337:
8327:
8323:
8313:
8309:
8299:
8295:
8285:
8275:
8252:
8248:
8244:
8234:
8230:
8225:
8217:
8213:
8196:
8192:
8188:
8178:
8174:
8157:
8153:
8149:
8144:HbE Portland II
8139:
8135:
8125:
8121:
8111:
8107:
8086:
8066:
7993:
7924:Alpha locus on
7893:
7879:
7849:
7844:
7835:oxygen toxicity
7811:
7699:ventilation (V)
7687:
7683:pulmonary shunt
7661:
7652:peak flow meter
7572:
7490:
7397:
7392:
7350:Wayback Machine
7339:Wayback Machine
7309:
7267:(12): a011627.
7202:
7181:
7133:
7115:
7114:
7113:
7098:
7097:
7093:
7086:
7084:Further reading
7081:
7080:
7070:
7068:
7055:
7054:
7050:
7040:
7038:
7027:
7023:
7016:
7002:
6998:
6967:
6963:
6956:
6940:
6936:
6891:
6887:
6850:
6846:
6805:(12): 6643–47.
6791:
6787:
6758:Eur. J. Biochem
6750:
6746:
6723:(15): 8875–81.
6709:
6705:
6696:
6694:
6651:
6647:
6638:
6636:
6623:
6622:
6618:
6573:
6569:
6524:
6520:
6489:
6485:
6454:
6450:
6427:
6423:
6384:
6380:
6327:
6323:
6294:(10): 2277–82.
6284:
6280:
6271:
6269:
6260:
6259:
6255:
6238:
6234:
6217:
6216:
6212:
6203:
6201:
6188:
6187:
6183:
6167:
6163:
6157:Wayback Machine
6147:
6143:
6114:
6110:
6106:at Medline Plus
6104:Wayback Machine
6095:
6091:
6052:
6048:
6042:Wayback Machine
6033:
6029:
6020:
6018:
6005:
6004:
6000:
5963:
5959:
5950:
5948:
5941:
5923:
5919:
5913:Wayback Machine
5904:
5900:
5886:Wayback Machine
5877:
5873:
5860:
5856:
5849:
5835:
5831:
5800:
5796:
5787:
5785:
5772:
5771:
5767:
5760:
5746:
5742:
5711:
5707:
5676:
5672:
5651:(3): R1376–83.
5640:
5636:
5629:
5617:
5616:
5612:
5601:
5599:
5595:
5588:
5574:
5570:
5553:
5549:
5537:
5535:
5514:
5510:
5503:
5489:
5485:
5446:
5442:
5411:
5407:
5344:
5340:
5277:
5273:
5203:
5196:
5135:
5126:
5079:
5072:
5017:
5010:
4957:
4953:
4946:
4932:
4928:
4905:(1–2): 83–162.
4891:
4887:
4871:
4867:
4858:
4856:
4845:
4841:
4832:
4830:
4821:
4820:
4816:
4810:Wayback Machine
4801:
4797:
4791:Wayback Machine
4782:
4775:
4736:
4732:
4726:Wayback Machine
4717:
4713:
4676:
4672:
4663:
4661:
4650:
4646:
4640:Wayback Machine
4631:
4627:
4621:Wayback Machine
4612:
4608:
4567:(12): 5675–79.
4553:
4549:
4540:
4538:
4531:
4515:
4511:
4505:Wayback Machine
4496:
4492:
4485:
4471:
4464:
4417:
4413:
4404:
4402:
4393:
4392:
4388:
4325:
4321:
4258:
4254:
4245:
4243:
4234:
4233:
4229:
4220:
4216:
4207:
4205:
4194:
4190:
4184:Wayback Machine
4175:
4171:
4162:
4160:
4145:
4138:
4129:
4127:
4114:
4113:
4109:
4100:
4098:
4085:
4084:
4080:
4071:
4069:
4026:
4022:
3983:(12): a011627.
3969:
3962:
3909:
3905:
3868:Protein Science
3860:
3856:
3833:
3829:
3781:
3777:
3767:
3765:
3745:
3738:
3723:
3719:
3710:
3708:
3704:
3693:
3689:
3688:
3684:
3669:
3665:
3655:
3653:
3640:
3636:
3627:
3625:
3611:
3607:
3598:
3596:
3582:
3578:
3541:
3537:
3502:
3501:
3497:
3488:
3486:
3473:
3469:
3452:
3451:
3447:
3408:
3401:
3392:
3390:
3377:
3376:
3372:
3315:
3302:
3269:(803237): 1–8.
3253:
3249:
3218:
3214:
3205:
3203:
3196:
3180:
3176:
3169:
3153:
3149:
3140:
3138:
3117:
3113:
3082:(12): 1325–28.
3068:
3064:
3019:
3015:
2974:
2967:
2960:
2944:
2940:
2933:
2902:
2898:
2891:
2874:
2870:
2865:
2860:
2859:
2853:
2849:
2845:
2840:
2836:
2809:
2770:
2766:
2752:
2748:
2743:
2738:
2730:
2725:Vaska's complex
2711:(with diatomic
2666:
2653:Medicine portal
2651:
2646:
2644:
2637:
2630:
2627:
2562:
2556:in the kidney.
2554:mesangial cells
2542:iron metabolism
2506:cerebral cortex
2496:neurons in the
2490:
2383:
2377:
2369:
2365:
2361:
2357:
2353:
2349:
2345:
2340:digestive tract
2338:. Instead of a
2328:giant tube worm
2277:
2273:
2228:
2215:
2193:
2189:
2185:
2173:
2169:
2064:
2058:
2056:Diagnostic uses
2020:
2016:
2008:
1999:
1933:iron deficiency
1919:
1884:
1853:Free hemoglobin
1849:red blood cells
1845:
1813:
1809:
1795:
1791:
1781:
1777:
1767:
1753:
1750:Hemoglobin H (β
1746:
1742:
1707:
1703:
1693:
1689:
1684:
1668:
1666:
1662:
1635:
1633:
1629:
1614:
1610:
1603:
1599:
1584:
1582:
1578:
1571:
1567:
1524:
1498:
1494:
1471:
1448:
1444:
1429:
1393:
1389:
1385:
1381:
1377:
1343:
1337:
1307:
1300:(S), including
1294:sulfur monoxide
1259:tobacco smoking
1255:
1227:
1218:carbon monoxide
1206:
1114:
1106:Channichthyidae
1083:
1071:magnetic fields
1040:
1033:
1013:
1009:
1001:
954:
946:
905:
901:
766:
734:proerythroblast
714:
703:
651:gene regulation
553:
428:
414:, is caused by
385:iron metabolism
377:mesangial cells
343:
324:
318:
291:
287:
283:
260:Channichthyidae
252:red blood cells
104:
86:
73:
67:
54:
46:
41:
28:
23:
22:
15:
12:
11:
5:
9072:
9062:
9061:
9056:
9051:
9046:
9029:
9028:
9026:
9025:
9024:
9023:
9016:Flow cytometry
9013:
9008:
9003:
8997:
8995:
8991:
8990:
8988:
8987:
8986:
8985:
8980:
8970:
8965:
8960:
8959:
8958:
8953:
8949:
8944:
8934:
8933:
8932:
8927:
8922:
8917:
8912:
8902:
8897:
8896:
8895:
8885:
8884:
8883:
8878:
8868:
8867:
8866:
8861:
8856:
8854:Reptilase time
8846:
8841:
8840:
8839:
8834:
8829:
8824:
8819:
8808:
8806:
8800:
8799:
8797:
8796:
8791:
8785:
8780:
8775:
8774:
8773:
8768:
8763:
8752:
8751:
8750:
8745:
8735:
8734:
8733:
8727:
8721:
8709:
8707:
8700:
8699:
8697:
8696:
8695:
8694:
8684:
8683:
8682:
8675:Platelet count
8672:
8671:
8670:
8665:
8655:
8654:
8653:
8652:
8651:
8646:
8641:
8636:
8621:
8616:
8610:
8608:
8602:
8601:
8591:
8590:
8583:
8576:
8568:
8559:
8558:
8550:
8547:
8546:
8544:
8543:
8538:
8537:
8536:
8531:
8520:
8518:
8514:
8513:
8510:
8509:
8506:
8505:
8503:
8502:
8496:
8494:
8488:
8487:
8485:
8484:
8479:
8474:
8473:
8472:
8461:
8459:
8450:
8446:
8445:
8442:
8441:
8439:
8438:
8436:Erythrocruorin
8433:
8427:
8425:
8421:
8420:
8418:
8417:
8412:
8406:
8404:
8400:
8399:
8397:
8396:
8394:Sulfhemoglobin
8391:
8382:
8377:
8371:
8369:
8365:
8364:
8361:
8360:
8358:
8357:
8353:
8349:
8343:
8339:
8335:
8329:
8325:
8321:
8315:
8311:
8307:
8301:
8297:
8293:
8287:
8283:
8277:
8273:
8266:
8264:
8258:
8257:
8254:
8253:
8251:
8250:
8246:
8242:
8236:
8232:
8228:
8223:
8219:
8215:
8211:
8204:
8202:
8198:
8197:
8195:
8194:
8190:
8186:
8180:
8176:
8172:
8165:
8163:
8159:
8158:
8156:
8155:
8151:
8147:
8141:
8137:
8133:
8130:HbE Portland I
8127:
8123:
8119:
8113:
8109:
8105:
8098:
8096:
8089:
8078:
8072:
8071:
8068:
8067:
8065:
8064:
8063:
8062:
8052:
8051:
8050:
8045:
8035:
8034:
8033:
8023:
8022:
8021:
8010:
8008:
7995:
7994:
7992:
7991:
7990:
7989:
7979:
7978:
7977:
7967:
7966:
7965:
7955:
7954:
7953:
7948:
7943:
7932:
7930:
7917:
7910:
7901:
7895:
7894:
7878:
7877:
7870:
7863:
7855:
7846:
7845:
7843:
7842:
7837:
7832:
7831:
7830:
7819:
7817:
7813:
7812:
7810:
7809:
7799:
7794:
7789:
7784:
7781:chloride shift
7774:
7771:Haldane effect
7768:
7763:
7758:
7749:
7744:
7739:
7734:
7729:
7724:
7719:
7718:
7717:
7712:
7701:
7695:
7693:
7689:
7688:
7686:
7685:
7680:
7675:
7669:
7667:
7663:
7662:
7660:
7659:
7654:
7649:
7644:
7639:
7637:
7631:
7630:
7628:FEV1/FVC ratio
7625:
7620:
7618:
7614:
7613:
7608:
7603:
7598:
7593:
7588:
7582:
7580:
7574:
7573:
7571:
7570:
7569:
7568:
7558:
7557:
7556:
7551:
7543:chemoreceptors
7539:
7538:
7537:
7532:
7520:
7519:
7518:
7513:
7500:
7498:
7492:
7491:
7489:
7488:
7483:
7482:
7481:
7476:
7471:
7463:
7458:
7453:
7451:elastic recoil
7448:
7443:
7438:
7433:
7428:
7427:
7426:
7421:
7416:
7405:
7403:
7399:
7398:
7391:
7390:
7383:
7376:
7368:
7362:
7361:
7352:
7329:
7320:
7308:
7307:External links
7305:
7304:
7303:
7252:
7223:
7206:
7200:
7185:
7179:
7166:
7137:
7131:
7112:
7111:
7106:
7100:
7099:
7088:
7087:
7085:
7082:
7079:
7078:
7048:
7021:
7014:
6996:
6977:(5744): 2160.
6961:
6954:
6934:
6905:(8): 1500–08.
6885:
6864:(9): 5668–76.
6844:
6785:
6744:
6703:
6645:
6616:
6581:Hum Brain Mapp
6567:
6538:(3): 645–654.
6518:
6483:
6448:
6421:
6378:
6321:
6278:
6253:
6232:
6229:on 2009-09-25.
6210:
6181:
6161:
6141:
6108:
6089:
6046:
6027:
5998:
5957:
5939:
5917:
5898:
5871:
5854:
5847:
5829:
5794:
5765:
5758:
5740:
5705:
5670:
5634:
5627:
5610:
5593:
5586:
5568:
5547:
5508:
5501:
5483:
5440:
5405:
5358:(7): 3773–77.
5338:
5291:(4): 2158–62.
5271:
5194:
5124:
5070:
5008:
4951:
4944:
4926:
4885:
4865:
4839:
4814:
4795:
4773:
4740:J Appl Physiol
4730:
4711:
4670:
4644:
4625:
4606:
4547:
4529:
4509:
4490:
4483:
4462:
4431:(7): 1266–72.
4411:
4386:
4319:
4252:
4227:
4214:
4188:
4169:
4136:
4107:
4078:
4020:
3960:
3903:
3854:
3827:
3775:
3736:
3717:
3682:
3663:
3634:
3605:
3591:. p. 43.
3576:
3535:
3495:
3467:
3464:on 2016-04-23.
3445:
3418:(2): 569–628.
3399:
3370:
3300:
3247:
3212:
3194:
3174:
3167:
3147:
3111:
3062:
3013:
2965:
2958:
2938:
2931:
2896:
2889:
2877:Wells, John C.
2867:
2866:
2864:
2861:
2858:
2857:
2851:
2843:
2834:
2745:
2744:
2742:
2739:
2737:
2734:
2733:
2732:
2728:
2722:
2721:- "blood clam"
2716:
2706:
2700:
2695:
2690:
2685:
2680:
2674:
2668:
2664:
2657:
2656:
2642:
2639:Biology portal
2626:
2623:
2561:
2558:
2550:alveolar cells
2489:
2486:
2485:
2484:
2481:
2475:
2474:
2466:
2460:
2459:
2452:
2450:Erythrocruorin
2446:
2445:
2433:Also known as
2431:
2425:
2424:
2421:
2415:
2414:
2411:
2405:
2404:
2400:
2394:
2393:
2389:
2379:Main article:
2376:
2373:
2367:
2363:
2359:
2355:
2351:
2347:
2343:
2336:volcanic vents
2275:
2271:
2227:
2224:
2220:pulse oximeter
2214:
2211:
2191:
2187:
2183:
2171:
2167:
2125:
2124:
2121:
2118:
2115:
2088:blood donation
2060:Main article:
2057:
2054:
2043:erythropoietin
2018:
2014:
2009:increases. In
2006:
1997:
1957:kidney failure
1917:
1883:
1880:
1844:
1841:
1840:
1839:
1829:
1822:
1815:
1811:
1807:
1801:
1793:
1789:
1783:
1779:
1775:
1769:
1765:
1759:
1751:
1748:
1744:
1740:
1714:
1713:
1705:
1701:
1695:
1691:
1687:
1682:
1678:
1664:
1660:
1646:
1645:
1631:
1627:
1617:
1616:
1612:
1608:
1605:
1601:
1597:
1594:
1580:
1576:
1573:
1569:
1565:
1523:
1520:
1496:
1492:
1469:
1458:oxygen tension
1446:
1442:
1427:
1406:to hemoglobin.
1396:
1395:
1391:
1387:
1383:
1379:
1375:
1336:
1333:
1305:
1254:
1251:
1225:
1205:
1202:
1130:protein chains
1113:
1110:
1089:diverged from
1082:
1079:
1052:pulse oximeter
1039:
1036:
1031:
1011:
1007:
999:
985:carbon dioxide
953:
950:
945:
942:
934:hydrogen bonds
910:, for a total
903:
899:
765:
762:
713:
710:
701:
696:Birds' unique
687:A. viridicuada
552:
549:
504:Claude Bernard
427:
424:
408:hemoglobinemia
373:alveolar cells
341:
334:carbon dioxide
322:
296:metalloprotein
219:
218:
215:
214:
206:
201:
197:
196:
188:
183:
179:
178:
170:
165:
161:
160:
157:
154:
146:
145:
139:
135:
134:
128:
124:
123:
113:metalloprotein
110:
106:
105:
65:
57:
56:
52:
37:
36:
26:
9:
6:
4:
3:
2:
9071:
9060:
9057:
9055:
9052:
9050:
9047:
9045:
9042:
9041:
9039:
9022:
9019:
9018:
9017:
9014:
9012:
9009:
9007:
9004:
9002:
8999:
8998:
8996:
8992:
8984:
8981:
8979:
8976:
8975:
8974:
8971:
8969:
8966:
8964:
8961:
8957:
8950:
8948:
8945:
8943:
8940:
8939:
8938:
8935:
8931:
8928:
8926:
8923:
8921:
8918:
8916:
8913:
8911:
8908:
8907:
8906:
8903:
8901:
8898:
8894:
8891:
8890:
8889:
8886:
8882:
8879:
8877:
8874:
8873:
8872:
8869:
8865:
8862:
8860:
8857:
8855:
8852:
8851:
8850:
8849:animal enzyme
8847:
8845:
8844:Bleeding time
8842:
8838:
8835:
8833:
8830:
8828:
8827:Thrombin time
8825:
8823:
8820:
8818:
8815:
8814:
8813:
8810:
8809:
8807:
8805:
8801:
8795:
8792:
8789:
8786:
8784:
8781:
8779:
8776:
8772:
8771:Mentzer index
8769:
8767:
8764:
8762:
8759:
8758:
8756:
8753:
8749:
8746:
8744:
8741:
8740:
8739:
8736:
8731:
8728:
8725:
8724:Plasma volume
8722:
8719:
8716:
8715:
8714:
8711:
8710:
8708:
8706:
8701:
8693:
8690:
8689:
8688:
8685:
8681:
8678:
8677:
8676:
8673:
8669:
8666:
8664:
8661:
8660:
8659:
8656:
8650:
8647:
8645:
8642:
8640:
8637:
8635:
8632:
8631:
8630:
8627:
8626:
8625:
8622:
8620:
8617:
8615:
8612:
8611:
8609:
8607:
8603:
8599:
8596:
8589:
8584:
8582:
8577:
8575:
8570:
8569:
8566:
8556:
8555:
8548:
8542:
8541:Methemalbumin
8539:
8535:
8532:
8530:
8527:
8526:
8525:
8522:
8521:
8519:
8515:
8501:
8500:Leghemoglobin
8498:
8497:
8495:
8493:
8489:
8483:
8480:
8478:
8475:
8471:
8468:
8467:
8466:
8463:
8462:
8460:
8458:
8454:
8451:
8447:
8437:
8434:
8432:
8431:Chlorocruorin
8429:
8428:
8426:
8422:
8416:
8415:Methemoglobin
8413:
8411:
8408:
8407:
8405:
8401:
8395:
8392:
8390:
8386:
8385:Oxyhemoglobin
8383:
8381:
8378:
8376:
8373:
8372:
8370:
8366:
8347:
8344:
8333:
8330:
8319:
8316:
8305:
8302:
8291:
8288:
8281:
8278:
8271:
8268:
8267:
8265:
8263:
8259:
8240:
8237:
8226:
8220:
8209:
8206:
8205:
8203:
8199:
8184:
8181:
8170:
8167:
8166:
8164:
8160:
8145:
8142:
8131:
8128:
8117:
8114:
8103:
8100:
8099:
8097:
8093:
8090:
8088:
8082:
8079:
8077:
8073:
8061:
8058:
8057:
8056:
8053:
8049:
8046:
8044:
8041:
8040:
8039:
8036:
8032:
8029:
8028:
8027:
8024:
8020:
8017:
8016:
8015:
8012:
8011:
8009:
8007:
8005:
8001:
7996:
7988:
7985:
7984:
7983:
7980:
7976:
7973:
7972:
7971:
7968:
7964:
7961:
7960:
7959:
7956:
7952:
7949:
7947:
7944:
7942:
7939:
7938:
7937:
7934:
7933:
7931:
7929:
7927:
7921:
7918:
7914:
7911:
7909:
7905:
7902:
7900:
7896:
7891:
7887:
7884:that contain
7883:
7876:
7871:
7869:
7864:
7862:
7857:
7856:
7853:
7841:
7838:
7836:
7833:
7829:
7826:
7825:
7824:
7823:high altitude
7821:
7820:
7818:
7816:Insufficiency
7814:
7807:
7803:
7800:
7798:
7795:
7793:
7790:
7788:
7787:oxyhemoglobin
7785:
7782:
7778:
7775:
7772:
7769:
7767:
7764:
7762:
7759:
7757:
7753:
7750:
7748:
7745:
7743:
7740:
7738:
7735:
7733:
7730:
7728:
7725:
7723:
7720:
7716:
7713:
7711:
7708:
7707:
7705:
7702:
7700:
7697:
7696:
7694:
7690:
7684:
7681:
7679:
7676:
7674:
7671:
7670:
7668:
7664:
7658:
7655:
7653:
7650:
7648:
7645:
7643:
7640:
7638:
7636:
7633:
7632:
7629:
7626:
7624:
7621:
7619:
7616:
7615:
7612:
7609:
7607:
7604:
7602:
7599:
7597:
7594:
7592:
7589:
7587:
7584:
7583:
7581:
7579:
7575:
7567:
7564:
7563:
7562:
7559:
7555:
7552:
7550:
7547:
7546:
7545:
7544:
7540:
7536:
7533:
7531:
7528:
7527:
7526:
7525:
7521:
7517:
7514:
7512:
7509:
7508:
7507:
7506:
7502:
7501:
7499:
7497:
7493:
7487:
7484:
7480:
7477:
7475:
7472:
7470:
7467:
7466:
7464:
7462:
7459:
7457:
7456:hysteresivity
7454:
7452:
7449:
7447:
7444:
7442:
7439:
7437:
7434:
7432:
7429:
7425:
7422:
7420:
7417:
7415:
7412:
7411:
7410:
7407:
7406:
7404:
7400:
7396:
7389:
7384:
7382:
7377:
7375:
7370:
7369:
7366:
7360:
7356:
7353:
7351:
7347:
7344:
7340:
7336:
7333:
7330:
7328:
7324:
7321:
7319:
7318:
7315:
7311:
7310:
7300:
7296:
7291:
7286:
7282:
7278:
7274:
7270:
7266:
7262:
7258:
7253:
7249:
7245:
7241:
7237:
7234:(2): 335–53.
7233:
7229:
7224:
7222:
7221:1-56072-907-4
7218:
7215:
7211:
7207:
7203:
7197:
7193:
7192:
7186:
7182:
7176:
7172:
7167:
7163:
7159:
7155:
7151:
7147:
7143:
7138:
7134:
7128:
7124:
7123:
7117:
7116:
7110:
7107:
7105:
7102:
7101:
7096:
7091:
7066:
7062:
7058:
7052:
7036:
7032:
7025:
7017:
7011:
7007:
7000:
6992:
6988:
6984:
6980:
6976:
6972:
6965:
6957:
6951:
6947:
6946:
6938:
6930:
6926:
6921:
6916:
6912:
6908:
6904:
6900:
6896:
6889:
6881:
6877:
6872:
6867:
6863:
6859:
6855:
6848:
6840:
6836:
6831:
6826:
6821:
6816:
6812:
6808:
6804:
6800:
6796:
6789:
6781:
6777:
6772:
6767:
6763:
6759:
6755:
6748:
6740:
6736:
6731:
6726:
6722:
6718:
6717:J. Biol. Chem
6714:
6707:
6692:
6688:
6684:
6680:
6676:
6672:
6668:
6664:
6660:
6656:
6649:
6634:
6630:
6626:
6620:
6612:
6608:
6603:
6598:
6594:
6590:
6586:
6582:
6578:
6571:
6563:
6559:
6555:
6551:
6546:
6541:
6537:
6533:
6529:
6522:
6514:
6510:
6506:
6502:
6498:
6494:
6487:
6479:
6475:
6471:
6467:
6464:(4): 289–99.
6463:
6459:
6452:
6444:
6440:
6437:(3): 123–27.
6436:
6432:
6425:
6417:
6413:
6409:
6405:
6401:
6397:
6394:(6): 541–60.
6393:
6389:
6382:
6374:
6370:
6365:
6360:
6356:
6352:
6348:
6344:
6340:
6336:
6332:
6325:
6317:
6313:
6309:
6305:
6301:
6297:
6293:
6289:
6282:
6267:
6263:
6257:
6250:
6246:
6242:
6236:
6228:
6224:
6220:
6214:
6200:on 2007-01-29
6199:
6195:
6191:
6185:
6179:
6175:
6171:
6165:
6158:
6154:
6151:
6145:
6136:
6131:
6127:
6123:
6119:
6112:
6105:
6101:
6098:
6093:
6085:
6081:
6077:
6073:
6069:
6065:
6062:(4): 317–20.
6061:
6057:
6050:
6043:
6039:
6036:
6031:
6016:
6012:
6008:
6002:
5994:
5990:
5985:
5980:
5976:
5972:
5968:
5961:
5946:
5942:
5936:
5932:
5928:
5921:
5914:
5910:
5907:
5902:
5895:
5891:
5887:
5883:
5880:
5875:
5869:
5868:
5863:
5858:
5850:
5844:
5840:
5833:
5825:
5821:
5817:
5813:
5810:(1): 558–67.
5809:
5805:
5798:
5783:
5779:
5775:
5769:
5761:
5755:
5751:
5744:
5736:
5732:
5728:
5724:
5720:
5716:
5709:
5701:
5697:
5693:
5689:
5686:(3): 731–42.
5685:
5681:
5674:
5666:
5662:
5658:
5654:
5650:
5646:
5638:
5630:
5624:
5620:
5614:
5608:
5604:
5597:
5589:
5583:
5579:
5572:
5565:
5561:
5557:
5551:
5544:
5533:
5529:
5525:
5521:
5520:
5512:
5504:
5498:
5494:
5487:
5479:
5475:
5471:
5467:
5463:
5459:
5455:
5451:
5444:
5436:
5432:
5428:
5424:
5421:(6): 212–13.
5420:
5416:
5409:
5401:
5397:
5392:
5387:
5383:
5379:
5374:
5369:
5365:
5361:
5357:
5353:
5349:
5342:
5334:
5330:
5325:
5320:
5316:
5312:
5307:
5302:
5298:
5294:
5290:
5286:
5282:
5275:
5267:
5263:
5259:
5255:
5250:
5245:
5241:
5237:
5233:
5229:
5225:
5221:
5217:
5213:
5209:
5201:
5199:
5190:
5186:
5181:
5176:
5172:
5168:
5164:
5160:
5156:
5152:
5149:(2): 469–78.
5148:
5144:
5140:
5133:
5131:
5129:
5120:
5116:
5112:
5108:
5104:
5100:
5096:
5092:
5088:
5084:
5077:
5075:
5066:
5062:
5057:
5052:
5047:
5042:
5038:
5034:
5030:
5026:
5022:
5015:
5013:
5004:
5000:
4995:
4990:
4986:
4982:
4978:
4974:
4971:(3): 803–12.
4970:
4966:
4962:
4955:
4947:
4941:
4937:
4930:
4922:
4918:
4913:
4908:
4904:
4900:
4896:
4889:
4883:
4879:
4875:
4869:
4854:
4850:
4843:
4829:on 2010-08-31
4828:
4824:
4818:
4811:
4807:
4804:
4799:
4792:
4788:
4785:
4784:"Hemoglobin."
4780:
4778:
4769:
4765:
4761:
4757:
4753:
4749:
4746:(2): 511–19.
4745:
4741:
4734:
4727:
4723:
4720:
4715:
4707:
4703:
4698:
4693:
4690:(2): 133–48.
4689:
4685:
4681:
4674:
4659:
4655:
4654:"Blood cells"
4648:
4641:
4637:
4634:
4629:
4622:
4618:
4615:
4614:"Hemoglobin."
4610:
4602:
4598:
4593:
4588:
4583:
4578:
4574:
4570:
4566:
4562:
4558:
4551:
4536:
4532:
4526:
4522:
4521:
4513:
4506:
4502:
4499:
4494:
4486:
4480:
4476:
4469:
4467:
4458:
4454:
4449:
4444:
4439:
4434:
4430:
4426:
4422:
4415:
4400:
4396:
4390:
4382:
4378:
4373:
4368:
4364:
4360:
4355:
4350:
4346:
4342:
4338:
4334:
4330:
4323:
4315:
4311:
4306:
4301:
4297:
4293:
4288:
4283:
4279:
4275:
4271:
4267:
4263:
4256:
4241:
4237:
4231:
4224:
4218:
4204:on 2007-12-15
4203:
4199:
4192:
4185:
4181:
4178:
4173:
4158:
4154:
4150:
4143:
4141:
4125:
4121:
4117:
4111:
4096:
4092:
4088:
4082:
4067:
4063:
4059:
4055:
4051:
4047:
4043:
4040:(4): 252–56.
4039:
4035:
4031:
4024:
4016:
4012:
4007:
4002:
3998:
3994:
3990:
3986:
3982:
3978:
3974:
3967:
3965:
3956:
3952:
3947:
3942:
3938:
3934:
3930:
3926:
3922:
3918:
3914:
3907:
3899:
3895:
3890:
3885:
3881:
3877:
3873:
3869:
3865:
3858:
3850:
3846:
3842:
3838:
3831:
3823:
3819:
3815:
3811:
3807:
3803:
3799:
3795:
3791:
3787:
3779:
3763:
3758:
3754:
3750:
3743:
3741:
3732:
3728:
3721:
3707:on 2008-04-10
3703:
3699:
3692:
3686:
3678:
3674:
3667:
3651:
3647:
3646:
3638:
3623:
3619:
3618:
3609:
3594:
3590:
3589:
3580:
3571:
3566:
3562:
3558:
3554:
3550:
3546:
3539:
3531:
3527:
3522:
3517:
3513:
3509:
3505:
3499:
3484:
3480:
3479:
3471:
3463:
3459:
3455:
3449:
3441:
3437:
3433:
3429:
3425:
3421:
3417:
3413:
3406:
3404:
3388:
3384:
3380:
3379:"Blood Tests"
3374:
3366:
3362:
3357:
3352:
3347:
3342:
3338:
3334:
3330:
3326:
3325:
3320:
3313:
3311:
3309:
3307:
3305:
3296:
3292:
3287:
3282:
3277:
3272:
3268:
3264:
3263:
3258:
3251:
3243:
3239:
3235:
3231:
3228:(4): 239–47.
3227:
3223:
3216:
3201:
3197:
3191:
3187:
3186:
3178:
3170:
3164:
3160:
3159:
3151:
3136:
3132:
3128:
3124:
3123:
3115:
3107:
3103:
3099:
3095:
3090:
3085:
3081:
3077:
3073:
3066:
3058:
3054:
3049:
3044:
3040:
3036:
3033:(4): 581–88.
3032:
3028:
3027:J Clin Invest
3024:
3017:
3009:
3005:
3001:
2997:
2993:
2989:
2985:
2981:
2980:
2972:
2970:
2961:
2955:
2951:
2950:
2942:
2934:
2928:
2924:
2923:
2918:
2914:
2910:
2906:
2905:Jones, Daniel
2900:
2892:
2886:
2882:
2878:
2872:
2868:
2847:
2838:
2830:
2764:
2760:
2756:
2750:
2746:
2726:
2723:
2720:
2717:
2714:
2710:
2709:Oxyhemoglobin
2707:
2704:
2703:Methemoglobin
2701:
2699:
2696:
2694:
2691:
2689:
2686:
2684:
2681:
2678:
2675:
2672:
2669:
2662:
2659:
2658:
2654:
2643:
2640:
2634:
2629:
2622:
2620:
2616:
2611:
2609:
2605:
2601:
2597:
2592:
2589:
2586:
2582:
2574:
2570:
2566:
2557:
2555:
2551:
2547:
2543:
2539:
2534:
2532:
2528:
2524:
2519:
2515:
2511:
2507:
2503:
2499:
2495:
2482:
2480:
2477:
2476:
2472:
2467:
2465:
2464:Leghemoglobin
2462:
2461:
2457:
2453:
2451:
2448:
2447:
2443:
2439:
2437:
2432:
2430:
2427:
2426:
2422:
2420:
2419:Chlorocruorin
2417:
2416:
2412:
2410:
2407:
2406:
2401:
2399:
2396:
2395:
2390:
2388:
2385:
2384:
2382:
2372:
2341:
2337:
2333:
2329:
2324:
2322:
2318:
2314:
2310:
2306:
2302:
2298:
2290:
2289:
2283:
2279:
2269:
2265:
2261:
2257:
2253:
2250:and the heme
2249:
2245:
2241:
2237:
2233:
2223:
2221:
2210:
2208:
2204:
2200:
2195:
2181:
2180:concentration
2177:
2165:
2160:
2156:
2154:
2150:
2145:
2141:
2139:
2135:
2131:
2128:
2122:
2119:
2116:
2113:
2112:
2111:
2109:
2105:
2101:
2097:
2093:
2089:
2085:
2081:
2073:
2068:
2063:
2053:
2050:
2048:
2044:
2040:
2036:
2035:cor pulmonale
2032:
2028:
2023:
2012:
2004:
2000:
1993:
1988:
1986:
1982:
1981:
1975:
1973:
1969:
1965:
1960:
1958:
1954:
1950:
1946:
1942:
1938:
1934:
1929:
1927:
1923:
1914:
1911:
1909:
1905:
1901:
1897:
1893:
1889:
1879:
1877:
1873:
1869:
1865:
1860:
1858:
1854:
1850:
1837:
1833:
1830:
1827:
1823:
1820:
1816:
1805:
1802:
1799:
1787:
1784:
1773:
1770:
1763:
1760:
1757:
1756:α thalassemia
1749:
1738:
1735:
1734:
1733:
1727:
1723:
1718:
1711:
1699:
1696:
1685:
1679:
1675:
1671:
1658:
1655:
1654:
1653:
1651:
1642:
1638:
1625:
1622:
1621:
1620:
1606:
1595:
1591:
1587:
1574:
1563:
1562:
1561:
1559:
1554:
1552:
1548:
1544:
1540:
1536:
1532:
1528:
1519:
1517:
1513:
1508:
1506:
1502:
1490:
1485:
1483:
1482:hydrogen bond
1479:
1475:
1466:
1463:
1459:
1455:
1450:
1449:in tissues).
1439:
1437:
1433:
1425:
1421:
1417:
1413:
1405:
1400:
1373:
1372:
1371:
1369:
1365:
1361:
1360:carbonic acid
1357:
1353:
1348:
1342:
1332:
1330:
1326:
1325:methemoglobin
1322:
1318:
1314:
1309:
1303:
1299:
1295:
1291:
1286:
1284:
1280:
1276:
1272:
1268:
1264:
1260:
1250:
1248:
1243:
1239:
1235:
1231:
1223:
1219:
1215:
1211:
1201:
1199:
1194:
1192:
1188:
1184:
1179:
1175:
1170:
1166:
1163:
1159:
1151:
1147:
1143:
1139:
1135:
1131:
1127:
1123:
1118:
1112:Cooperativity
1109:
1107:
1102:
1100:
1096:
1092:
1088:
1078:
1076:
1072:
1068:
1063:
1061:
1057:
1053:
1049:
1045:
1035:
1029:
1025:
1021:
1016:
1005:
997:
993:
988:
986:
982:
978:
974:
970:
966:
962:
958:
957:Oxyhemoglobin
952:Oxyhemoglobin
949:
941:
939:
935:
931:
927:
922:
920:
915:
913:
909:
897:
893:
888:
886:
881:
877:
876:methemoglobin
873:
869:
864:
861:
859:
855:
851:
847:
843:
839:
835:
831:
827:
823:
818:
816:
812:
808:
804:
801:
797:
793:
788:
786:
785:alpha helices
782:
774:
770:
761:
759:
755:
754:ribosomal RNA
751:
747:
743:
739:
735:
731:
727:
723:
719:
709:
705:
699:
694:
692:
688:
684:
680:
676:
667:
662:
658:
656:
652:
648:
644:
640:
636:
635:
630:
626:
622:
618:
615:
611:
607:
603:
602:
597:
596:
591:
590:
585:
580:
578:
574:
570:
566:
562:
558:
548:
546:
542:
538:
534:
533:
528:
527:
522:
521:
516:
512:
507:
505:
502:
497:
495:
491:
487:
483:
479:
474:
472:
467:
462:
460:
456:
452:
444:
440:
436:
432:
423:
421:
417:
413:
409:
404:
402:
398:
394:
393:leghemoglobin
388:
386:
382:
378:
374:
370:
366:
362:
357:
355:
351:
347:
344:binds to the
340:, in which CO
339:
335:
330:
328:
316:
312:
307:
305:
301:
300:chromoprotein
297:
281:
277:
273:
269:
265:
261:
257:
254:. Almost all
253:
249:
245:
241:
237:
233:
229:
225:
213:
210:
207:
205:
202:
199:
198:
195:
192:
189:
187:
184:
181:
180:
177:
174:
171:
169:
166:
163:
162:
158:
155:
152:
151:
147:
143:
140:
136:
132:
129:
125:
122:
118:
117:chromoprotein
114:
111:
107:
103:
102:
99:
93:
89:
84:
80:
76:
70:
63:
58:
49:
44:
38:
33:
30:
19:
8937:Fibrinolysis
8848:
8713:Blood volume
8613:
8551:
8529:Cytochrome b
8491:
8470:Metmyoglobin
8456:
8384:
8261:
8087:development:
8084:
8054:
8037:
8025:
8013:
7998:
7981:
7969:
7957:
7935:
7923:
7907:
7890:hemoproteins
7746:
7727:gas exchange
7692:Interactions
7617:calculations
7578:Lung volumes
7541:
7522:
7503:
7474:constriction
7436:respirometer
7312:
7264:
7260:
7231:
7227:
7209:
7190:
7170:
7145:
7141:
7122:Biochemistry
7121:
7094:
7069:. Retrieved
7063:. Montréal.
7060:
7051:
7039:. Retrieved
7033:. CBC News.
7024:
7005:
6999:
6974:
6970:
6964:
6944:
6937:
6902:
6898:
6888:
6861:
6857:
6847:
6802:
6798:
6788:
6761:
6757:
6747:
6720:
6716:
6706:
6695:. Retrieved
6662:
6658:
6648:
6637:. Retrieved
6628:
6619:
6587:(1): 14–23.
6584:
6580:
6570:
6535:
6531:
6521:
6496:
6492:
6486:
6461:
6457:
6451:
6434:
6430:
6424:
6391:
6387:
6381:
6338:
6334:
6324:
6291:
6287:
6281:
6270:. Retrieved
6256:
6240:
6235:
6227:the original
6222:
6213:
6202:. Retrieved
6198:the original
6193:
6184:
6169:
6164:
6144:
6125:
6121:
6111:
6092:
6059:
6055:
6049:
6030:
6019:. Retrieved
6010:
6001:
5974:
5970:
5960:
5949:. Retrieved
5930:
5920:
5901:
5893:
5889:
5874:
5865:
5857:
5838:
5832:
5807:
5803:
5797:
5786:. Retrieved
5777:
5768:
5752:. Elsevier.
5749:
5743:
5718:
5714:
5708:
5683:
5679:
5673:
5648:
5644:
5637:
5619:Biochemistry
5618:
5613:
5596:
5577:
5571:
5555:
5550:
5542:
5536:. Retrieved
5518:
5511:
5492:
5486:
5453:
5449:
5443:
5418:
5414:
5408:
5355:
5351:
5341:
5288:
5284:
5274:
5215:
5211:
5146:
5142:
5086:
5082:
5028:
5024:
4968:
4964:
4954:
4935:
4929:
4902:
4898:
4888:
4873:
4868:
4857:. Retrieved
4842:
4831:. Retrieved
4827:the original
4817:
4798:
4743:
4739:
4733:
4714:
4687:
4683:
4673:
4662:. Retrieved
4647:
4628:
4609:
4564:
4560:
4550:
4539:. Retrieved
4519:
4512:
4493:
4474:
4428:
4424:
4414:
4403:. Retrieved
4389:
4336:
4332:
4322:
4269:
4265:
4255:
4244:. Retrieved
4230:
4222:
4217:
4206:. Retrieved
4202:the original
4196:Uthman, Ed.
4191:
4172:
4161:. Retrieved
4152:
4128:. Retrieved
4119:
4110:
4099:. Retrieved
4090:
4081:
4070:. Retrieved
4037:
4033:
4023:
3980:
3976:
3920:
3916:
3906:
3871:
3867:
3857:
3840:
3836:
3830:
3789:
3785:
3778:
3766:. Retrieved
3752:
3730:
3726:
3720:
3709:. Retrieved
3702:the original
3697:
3685:
3676:
3672:
3666:
3654:. Retrieved
3644:
3637:
3626:. Retrieved
3615:
3608:
3597:. Retrieved
3586:
3579:
3552:
3548:
3538:
3511:
3507:
3498:
3487:. Retrieved
3477:
3470:
3462:the original
3457:
3448:
3415:
3412:Physiol. Rev
3411:
3391:. Retrieved
3382:
3373:
3328:
3322:
3266:
3260:
3250:
3225:
3221:
3215:
3204:. Retrieved
3184:
3177:
3157:
3150:
3139:. Retrieved
3121:
3114:
3079:
3076:Br J Anaesth
3075:
3065:
3030:
3026:
3016:
2983:
2977:
2948:
2941:
2920:
2917:Esling, John
2913:Setter, Jane
2909:Roach, Peter
2899:
2880:
2871:
2846:
2837:
2762:
2758:
2754:
2749:
2688:Delta globin
2614:
2612:
2603:
2593:
2578:
2568:
2535:
2531:neuromelanin
2526:
2518:dopaminergic
2494:dopaminergic
2491:
2434:
2331:
2325:
2294:
2286:
2229:
2216:
2196:
2161:
2157:
2146:
2142:
2136:
2132:
2129:
2126:
2077:
2051:
2027:polycythemia
2024:
1989:
1978:
1976:
1961:
1944:
1940:
1930:
1915:
1912:
1885:
1876:transferrins
1861:
1846:
1836:hemoglobin S
1826:hemoglobin C
1804:Hemoglobin E
1786:Hemoglobin C
1772:Hemoglobin S
1737:Hemoglobin D
1731:
1725:
1721:
1698:Hemoglobin F
1681:Hemoglobin A
1657:Hemoglobin A
1647:
1624:Hemoglobin F
1619:In fetuses:
1618:
1555:
1525:
1512:nitric oxide
1509:
1486:
1467:
1462:heterotropic
1461:
1451:
1440:
1431:
1409:
1346:
1344:
1320:
1310:
1287:
1275:CO poisoning
1256:
1247:vasodilatory
1238:Nitric oxide
1230:nitric oxide
1207:
1195:
1186:
1171:
1167:
1155:
1103:
1098:
1094:
1084:
1075:diamagnetism
1067:paramagnetic
1064:
1041:
1024:paramagnetic
1017:
996:relaxed form
995:
991:
989:
956:
955:
947:
930:salt bridges
923:
916:
896:hemoglobin A
895:
889:
865:
862:
826:heterocyclic
819:
789:
778:
738:reticulocyte
718:mitochondria
715:
706:
695:
686:
682:
671:
647:thalassemias
632:
619:
613:
609:
605:
599:
593:
587:
584:hemoglobin A
581:
565:polypeptides
554:
530:
524:
518:
514:
510:
508:
501:physiologist
498:
490:John Kendrew
475:
463:
454:
450:
447:
420:blood plasma
410:, a form of
405:
389:
358:
350:nitric oxide
346:heme protein
331:
308:
235:
231:
227:
223:
222:
153:Subunit name
109:Protein type
96:
74:
68:
47:
42:
29:
9049:Hemoglobins
8804:Coagulation
8783:Haptoglobin
8598:blood tests
8477:Neuroglobin
8403:Other human
8116:HbE Gower 2
8102:HbE Gower 1
7766:Bohr effect
7666:Circulation
7402:Respiration
7314:Proteopedia
7071:February 1,
7041:February 1,
4120:uniprot.org
4091:uniprot.org
3656:26 February
2698:Hemoprotein
2677:Chlorophyll
2546:macrophages
2538:antioxidant
2510:hippocampus
2471:nitrogenase
2442:sea squirts
2409:Hemerythrin
2403:oxygenated.
2313:crustaceans
2207:BOLD signal
2164:blood sugar
2080:blood tests
2041:, too much
1968:thalassemia
1941:hypochromic
1436:root effect
1424:Bohr effect
1364:bicarbonate
1352:Bohr effect
1323:globin" or
1263:exhaust gas
1253:Competitive
1020:diamagnetic
981:Ventilation
848:ring of F8
811:globin fold
807:alpha-helix
758:vasculature
742:bone marrow
679:Pleistocene
569:amino acids
515:haemoglobin
381:antioxidant
369:macrophages
352:bound to a
256:vertebrates
242:containing
228:haemoglobin
138:Cofactor(s)
98:Proteopedia
18:Haemoglobin
9038:Categories
9001:Blood film
8837:Fibrinogen
8619:Hematocrit
8614:Hemoglobin
8595:Hematology
8524:Cytochrome
8482:Cytoglobin
8262:pathology:
8085:stages of
8000:Beta locus
7908:Hemoglobin
7828:death zone
7747:hemoglobin
7642:spirometry
7601:dead space
7554:peripheral
7479:dilatation
7465:bronchial
7446:compliance
7419:exhalation
7414:inhalation
7327:anemia.org
7317:Hemoglobin
7228:J Mol Biol
7142:Am Heart J
7095:Hemoglobin
6697:2013-11-10
6665:(1): 1–4.
6639:2016-11-03
6499:: 715–54.
6272:2007-12-26
6249:1416001417
6204:2013-09-05
6178:0781719933
6128:(2): 109.
6097:Hemoglobin
6021:2015-10-28
5951:2016-02-18
5892:, stating
5788:2008-10-12
5721:: 161–79.
5564:1572599316
5538:2019-05-04
4882:0470129301
4859:2012-03-20
4833:2010-07-06
4719:Hemoglobin
4664:2020-03-27
4541:2016-02-18
4405:2007-12-26
4246:2010-05-02
4208:2007-12-26
4163:2008-10-12
4130:2020-03-10
4101:2020-03-10
4072:2019-12-26
3843:: 165–83.
3711:2008-10-12
3679:: 172–218.
3628:2021-11-30
3599:2021-11-30
3489:2020-06-16
3393:2019-04-27
3206:2016-01-09
3158:Physiology
3141:2019-05-04
2736:References
2731:reversibly
2598:created a
2571:(2005) by
2502:astrocytes
2479:Coboglobin
2456:earthworms
2438:chromagens
2398:Hemocyanin
2319:and giant
2268:arthropods
2266:and other
2236:protozoans
2138:Hematocrit
1980:porphyrias
1945:microcytic
1724:, (1976).
1575:Gower 2 (α
1564:Gower 1 (ζ
1539:population
1335:Allosteric
1296:(SO), and
1191:hyperbolic
1048:wavelength
994:(T) and a
936:, and the
880:superoxide
870:or in the
868:ferrous Fe
858:octahedron
824:held in a
800:prosthetic
573:translated
511:hemoglobin
482:Max Perutz
466:Otto Funke
435:Max Perutz
401:leguminous
315:dry weight
280:metabolism
224:Hemoglobin
133:-transport
101:Hemoglobin
35:Hemoglobin
8952:Plasmin-α
8552:see also
8465:Myoglobin
8368:Compounds
8239:HbF/Fetal
8169:HbF/Fetal
8095:Embryonic
8076:Tetramers
7704:Perfusion
7359:vimeo.com
7281:2157-1422
6991:190178048
6554:8750-7587
6316:205541592
5879:hypoxemia
5382:0027-8424
5315:0027-8424
5266:218761566
5240:1476-4687
5171:1095-9513
4363:0027-8424
4296:0027-8424
4054:0002-7685
3997:2157-1422
3937:1046-6673
3733:: 133–40.
3673:Z Rat Med
2850:This Hb A
2679:(Mg heme)
2600:sculpture
2585:porphyrin
2387:Myoglobin
2011:diabetics
1949:hemolysis
1900:hypoxemia
1864:bilirubin
1722:Wood W.G.
1644:).
1593:).
1551:pathology
1531:embryonic
1220:(CO) and
1198:resonance
1183:sigmoidal
1162:imidazole
1158:porphyrin
1150:histidine
1146:histidine
1002:and high
924:The four
872:ferric Fe
850:histidine
846:imidazole
830:porphyrin
815:myoglobin
730:ribosomes
712:Synthesis
643:mechanism
621:Mutations
509:The name
494:myoglobin
453:× 16000 (
443:myoglobin
397:anaerobic
8757:testing
8424:Nonhuman
7916:Subunits
7882:Proteins
7715:V/Q scan
7346:Archived
7335:Archived
7299:23209182
7248:16368110
7162:16368297
7065:Archived
7035:Archived
6929:18448584
6880:16407281
6839:10359765
6780:15265029
6691:Archived
6687:34214741
6633:Archived
6611:11870923
6562:28663373
6513:11701529
6478:18539160
6443:10916704
6408:10408656
6308:21666449
6266:Archived
6153:Archived
6100:Archived
6084:12771673
6038:Archived
6015:Archived
6011:ngsp.org
5945:Archived
5909:Archived
5882:Archived
5824:16115609
5782:Archived
5665:17626121
5532:Archived
5528:30855920
5470:19837879
5400:11259676
5258:32461643
5189:22846683
5065:26508205
4921:16005052
4853:Archived
4806:Archived
4787:Archived
4768:15468862
4760:11160049
4722:Archived
4658:Archived
4636:Archived
4617:Archived
4535:Archived
4501:Archived
4399:Archived
4381:15353580
4314:24297909
4240:Archived
4180:Archived
4157:Archived
4124:Archived
4095:Archived
4066:Archived
4062:84499907
4015:23209182
3955:18448584
3898:29607556
3849:13734651
3814:18990801
3768:25 March
3650:Archived
3622:Archived
3617:animals"
3593:Archived
3530:30330061
3483:Archived
3440:10863037
3432:11274340
3387:Archived
3365:19717439
3295:25431740
3200:Archived
3135:Archived
3131:30855920
3106:10029560
3057:13999462
3008:29978182
3000:16651546
2919:(eds.).
2907:(2011).
2879:(2008).
2625:See also
2436:vanadium
2429:Vanabins
2354:O and CO
2321:annelids
2309:molluscs
2305:nematode
2232:bacteria
1953:jaundice
1872:ferritin
1650:neonates
1505:placenta
1279:headache
1216:such as
1122:monomers
1087:lampreys
1056:cyanosis
892:tetramer
842:nitrogen
792:molecule
720:and the
551:Genetics
437:won the
304:globulin
127:Function
121:globulin
95:
8947:D-Dimer
7899:Globins
7840:hypoxia
7761:2,3-BPG
7549:central
7524:medulla
7496:Control
7290:3543078
6971:Science
6920:2488266
6807:Bibcode
6739:8621529
6667:Bibcode
6602:6871837
6458:Methods
6416:1092056
6373:9232855
6364:1691965
6343:Bibcode
6076:6741458
5993:8710285
5971:Nursing
5735:3288089
5700:6492161
5607:YouTube
5435:2763333
5360:Bibcode
5333:6929543
5293:Bibcode
5249:8259614
5220:Bibcode
5180:4306229
5151:Bibcode
5119:2979887
5111:1089897
5091:Bibcode
5056:4629386
5033:Bibcode
5003:8386018
4994:1262394
4973:Bibcode
4706:9564432
4601:8650150
4569:Bibcode
4457:5794250
4341:Bibcode
4305:3870697
4274:Bibcode
4006:3543078
3946:2488266
3889:5980623
3822:4208282
3794:Bibcode
3588:Beddoes
3557:Bibcode
3521:5763191
3356:2732704
3333:Bibcode
3286:4241286
3242:9435331
3098:7317251
2863:Sources
2759:globule
2602:called
2594:Artist
2504:in the
2362:S and O
2307:worms,
2264:insects
2256:muscles
2248:globins
2244:ligands
1992:glucose
1908:hypoxia
1868:kidneys
1558:embryos
1491:(HbF, α
1368:protons
1345:Carbon
1313:ferrous
1298:sulfide
1290:cyanide
1060:hypoxia
1004:2,3 BPG
969:alveoli
908:daltons
838:methine
834:pyrrole
775:b group
746:nucleus
740:in the
736:to the
722:cytosol
675:Mammoth
666:UniProt
631:called
537:subunit
363:of the
321:mL of O
311:mammals
240:protein
238:) is a
209:Chr. 11
191:Chr. 16
173:Chr. 16
8492:plant:
8457:human:
7951:pseudo
7409:breath
7297:
7287:
7279:
7246:
7219:
7198:
7177:
7160:
7129:
7092:about
7012:
6989:
6952:
6927:
6917:
6878:
6837:
6827:
6778:
6737:
6685:
6609:
6599:
6560:
6552:
6511:
6476:
6441:
6414:
6406:
6371:
6361:
6314:
6306:
6247:
6176:
6082:
6074:
5991:
5937:
5845:
5822:
5756:
5733:
5698:
5663:
5625:
5584:
5562:
5526:
5499:
5478:906177
5476:
5468:
5433:
5398:
5388:
5380:
5331:
5324:348671
5321:
5313:
5264:
5256:
5246:
5238:
5212:Nature
5187:
5177:
5169:
5117:
5109:
5083:Nature
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