111:
119:
254:(hence, its name), is one of twenty of the most common amino acids and was the first amino acid to be isolated. While ovotransferrin identifies with its family, there are two types of ovotransferrin proteins: apo and holo. Apo-Ovotransferrin is deprived of iron and holo-Ovotransferrin is saturated with iron. Because the apo-ovotransferrin is iron-deprived, it is easily destroyed by physical and chemical treatments.
29:
282:
Numerous studies have identified dual anti-osteoporotic properties of ovotransferrin, both reducing bone resorption and promoting bone formation. Beyond this, ovotransferrin shows promise as a drug carrier with potential applications in cancer treatment. Indeed, ovotransferrin alone is toxic to
165:
family, ovotransferrin has been found to possess antibacterial and antioxydant and immunomodulatory properties, arising primarily through its iron (Fe3+) binding capacity by locking away a key biochemical component necessary for micro-organismal survival. Bacteria starved of iron are rendered
198:
of animal serum. It has a binding log of 15 at a pH of 7 or above, meaning that the iron binding capacity of ovotransferrin rapidly decreased at a pH that is less than 6. This family is also known for their role in cell maturation by transporting essential nutrients to developing
274:(IDA). Ovotransferrin showed superior physiological iron delivery over lactoferrin in a gastric barrier model. This data holds much promise for ovotransferrin's use in food supplements, with dual functionality as both antimicrobial and iron delivery mechanism.
218:
The primary sequence of ovotransferrin is similar to that of many serum transferrins found in other species. Recently, scientists have discovered a blood serum transferrin in humans, that binds iron like ovotransferrin and which shows 50%
227:
content. At the C- lobe, human serum has two N-glycans while the hen ovotransferrin has a single N-glycan. Consequently, structurally this protein differs from its serum counterpart because of its
270:
in its capability to deliver iron without accumulation or inducing gastric irritability, rendering ovotransferrin as an excellent potential iron carrier for the treatment of
235:(formation of chemical bonds) that occurs in living organisms. This process is determined by the structure of the protein backbone and the carbohydrate attachment site.
1004:
262:
Biologically, conalbumin isolates and sequesters metallic contaminants in the egg white. Ovotransferrin is functionally and structurally analogous to mammalian
555:
Lee N, Cheng J, Enomoto T, Nakano YO (December 2009). "One peptide derived from hen ovotransferrin as pro-drug to inhibit angiotensin converting enzyme".
1136:
520:
Ibrahim HR, Kiyono T (December 2009). "Novel anticancer activity of the autocleaved ovotransferrin against human colon and breast cancer cells".
584:"The Utility of Ovotransferrin and Ovotransferrin-Derived Peptides as Possible Candidates in the Clinical Treatment of Cardiovascular Diseases"
668:
231:
pattern. These proteins are said to be glycosylated because they have carbohydrates attached to them. Glycosylation is the most common
361:
283:
cancer cells in-vitro. Its antioxidant and anti-inflammatory properties may also make ovotransferrin a viable treatment for
48:
661:
1115:
194:. Disulfide groups stabilize the tertiary structures of proteins. Transferrins are iron binding proteins and
846:
317:"OVOTRANSFERRIN: The nutraceutical protein with antimicrobial, antioxidant and immunomodulatory properties"
654:
485:
Shang N, Wu J (March 2018). "Egg White
Ovotransferrin Shows Osteogenic Activity in Osteoblast Cells".
1163:
1110:
721:
640:
385:"The Nutraceutical Properties of Ovotransferrin and Its Potential Utilization as a Functional Food"
436:"Ovotransferrin Supplementation Improves the Iron Absorption: An In Vitro Gastro-Intestinal Model"
1168:
1158:
781:
731:
717:
284:
271:
807:
232:
195:
1064:
880:
88:
8:
1059:
999:
745:
735:
725:
334:
Wu J, Acero-Lopez A (2012). "Ovotransferrin: Structure, bioactivities, and preparation".
211:
to the developing embryo. Because they bind to iron, this makes it difficult for harmful
183:
145:, of which ovotransferrin is the most heat reliable. It has a molecular weight of 76,000
238:
In addition, ovotransferrin is glycosylated by the N-linkage to the amino acid known as
1085:
977:
610:
583:
462:
435:
411:
384:
220:
636:
369:
316:
1094:
994:
937:
615:
537:
502:
467:
434:
Galla R, Grisenti P, Farghali M, Saccuman L, Ferraboschi P, Uberti F (October 2021).
416:
162:
677:
605:
595:
564:
529:
494:
457:
447:
406:
396:
343:
191:
347:
836:
757:
266:
A recent study has shown superior performance of ovotransferrin when compared to
175:
452:
178:
in a way that forms two lobes (N- and C- terminals) and each lobe consists of a
98:
952:
909:
826:
697:
1152:
1069:
1051:
989:
947:
943:
775:
498:
228:
204:
146:
110:
568:
741:
685:
619:
600:
541:
506:
471:
420:
224:
179:
153:. Ovotransferrin makes up approximately 13% of egg albumen (in contrast to
134:
1100:
1090:
982:
933:
870:
851:
811:
800:
768:
296:
267:
263:
158:
69:
215:
to be nutritionally satisfied with them so it acts as an antimicrobial.
1031:
239:
150:
64:
533:
401:
223:
to ovotransferrin, i.e., they have similar amino acid composition and
1036:
1023:
895:
875:
251:
187:
154:
138:
646:
166:
incapable of moving, making ovotransferrin a potent bacteriostatic.
917:
885:
688:
247:
212:
1014:
957:
890:
383:
Giansanti F, Leboffe L, Angelucci F, Antonini G (November 2015).
382:
142:
118:
1041:
707:
243:
200:
28:
1105:
433:
208:
554:
182:. Each lobe is then divided into two domains of 160
250:on the amino acid. Asparagine, found abundantly in
1150:
581:
582:Chen S, Jiang H, Peng H, Wu X, Fang J (2018).
277:
662:
519:
333:
246:, the carbohydrate chain, is attached to the
141:. Egg white albumen is composed of multiple
157:, which comprises 54%). As a member of the
669:
655:
522:Journal of Agricultural and Food Chemistry
487:Journal of Agricultural and Food Chemistry
27:
1137:disorders of globin and globulin proteins
639:at the U.S. National Library of Medicine
609:
599:
588:Oxidative Medicine and Cellular Longevity
461:
451:
410:
400:
257:
186:. Its structure also consists of fifteen
117:
109:
484:
1151:
676:
650:
13:
14:
1180:
630:
557:Journal of Food and Drug Analysis
203:. Ovotransferrin functions as an
1116:Extracellular matrix protein 1
575:
548:
513:
478:
427:
376:
354:
327:
309:
1:
348:10.1016/j.foodres.2011.07.012
302:
847:Sex hormone-binding globulin
169:
7:
453:10.3390/biomedicines9111543
336:Food Research International
290:
278:Role in disease and therapy
16:Protein found in egg whites
10:
1185:
1128:
1111:Vitamin D-binding protein
1078:
1050:
1022:
1013:
970:
926:
908:
861:
834:
825:
790:
755:
705:
696:
684:
94:
84:
79:
75:
63:
55:
43:
38:
26:
21:
722:Alpha 1-antichymotrypsin
641:Medical Subject Headings
499:10.1021/acs.jafc.8b00069
1005:7S seed storage protein
782:Retinol binding protein
569:10.38212/2224-6614.2505
190:crosslinks and no free
149:and contains about 700
285:cardiovascular disease
272:Iron-deficiency anemia
258:Function and mechanism
123:
115:
808:alpha-2-Macroglobulin
233:covalent modification
207:agent and transports
196:acute phase reactants
121:
113:
1065:Bovine serum albumin
881:Beta-2 microglobulin
601:10.1155/2017/6504518
1060:Human serum albumin
1000:11S globulin family
746:Heparin cofactor II
736:Alpha 2-antiplasmin
726:Alpha 1-antitrypsin
563:(23): 11383–11390.
528:(23): 11383–11390.
242:, meaning that the
184:amino acid residues
1086:C-reactive protein
978:Beta-lactoglobulin
174:Ovotransferrin is
124:
116:
1146:
1145:
1124:
1123:
1095:Alpha-lactalbumin
995:Alpha-lactalbumin
966:
965:
938:Fetal fibronectin
904:
903:
821:
820:
678:Globular proteins
534:10.1021/jf902638e
493:(11): 2775–2782.
402:10.3390/nu7115453
395:(11): 9105–9115.
192:sulfhydryl groups
163:metalloproteinase
139:egg white albumen
108:
107:
104:
103:
1176:
1164:Storage proteins
1020:
1019:
864:
840:
837:carrier proteins
832:
831:
793:
761:
758:carrier proteins
711:
703:
702:
694:
693:
671:
664:
657:
648:
647:
624:
623:
613:
603:
579:
573:
572:
552:
546:
545:
517:
511:
510:
482:
476:
475:
465:
455:
431:
425:
424:
414:
404:
380:
374:
373:
368:. Archived from
358:
352:
351:
331:
325:
324:
313:
77:
76:
51:
31:
19:
18:
1184:
1183:
1179:
1178:
1177:
1175:
1174:
1173:
1149:
1148:
1147:
1142:
1141:
1120:
1074:
1046:
1009:
971:Other globulins
962:
922:
918:Immunoglobulins
900:
862:
857:
854:
835:
817:
791:
786:
756:
751:
706:
698:Alpha globulins
680:
675:
633:
628:
627:
580:
576:
553:
549:
518:
514:
483:
479:
432:
428:
381:
377:
360:
359:
355:
332:
328:
315:
314:
310:
305:
293:
280:
260:
172:
47:
34:
17:
12:
11:
5:
1182:
1172:
1171:
1169:Avian proteins
1166:
1161:
1159:Blood proteins
1144:
1143:
1140:
1139:
1130:
1129:
1126:
1125:
1122:
1121:
1119:
1118:
1113:
1108:
1103:
1098:
1088:
1082:
1080:
1076:
1075:
1073:
1072:
1067:
1062:
1056:
1054:
1048:
1047:
1045:
1044:
1039:
1034:
1028:
1026:
1017:
1011:
1010:
1008:
1007:
1002:
997:
992:
987:
986:
985:
974:
972:
968:
967:
964:
963:
961:
960:
955:
953:Transcobalamin
950:
941:
930:
928:
924:
923:
921:
920:
914:
912:
910:Gamma globulin
906:
905:
902:
901:
899:
898:
893:
888:
883:
878:
873:
867:
865:
859:
858:
856:
855:
849:
843:
841:
829:
827:Beta globulins
823:
822:
819:
818:
816:
815:
804:
796:
794:
788:
787:
785:
784:
779:
772:
764:
762:
753:
752:
750:
749:
739:
729:
714:
712:
700:
691:
682:
681:
674:
673:
666:
659:
651:
645:
644:
632:
631:External links
629:
626:
625:
574:
547:
512:
477:
426:
375:
372:on 2011-07-16.
353:
342:(2): 480–487.
326:
321:Bioseutica B.V
307:
306:
304:
301:
300:
299:
292:
289:
279:
276:
259:
256:
171:
168:
127:Ovotransferrin
122:Basic N-glycan
106:
105:
102:
101:
96:
92:
91:
86:
82:
81:
73:
72:
67:
61:
60:
57:
53:
52:
45:
41:
40:
36:
35:
32:
24:
23:
22:Ovotransferrin
15:
9:
6:
4:
3:
2:
1181:
1170:
1167:
1165:
1162:
1160:
1157:
1156:
1154:
1138:
1135:
1132:
1131:
1127:
1117:
1114:
1112:
1109:
1107:
1104:
1102:
1099:
1096:
1092:
1089:
1087:
1084:
1083:
1081:
1077:
1071:
1068:
1066:
1063:
1061:
1058:
1057:
1055:
1053:
1052:Serum albumin
1049:
1043:
1040:
1038:
1035:
1033:
1030:
1029:
1027:
1025:
1021:
1018:
1016:
1012:
1006:
1003:
1001:
998:
996:
993:
991:
990:Thyroglobulin
988:
984:
981:
980:
979:
976:
975:
973:
969:
959:
956:
954:
951:
949:
948:Microglobulin
945:
944:Macroglobulin
942:
939:
935:
932:
931:
929:
925:
919:
916:
915:
913:
911:
907:
897:
894:
892:
889:
887:
884:
882:
879:
877:
874:
872:
869:
868:
866:
860:
853:
850:
848:
845:
844:
842:
838:
833:
830:
828:
824:
813:
809:
805:
802:
798:
797:
795:
789:
783:
780:
777:
776:Ceruloplasmin
773:
770:
766:
765:
763:
759:
754:
747:
743:
740:
737:
733:
730:
727:
723:
719:
716:
715:
713:
709:
704:
701:
699:
695:
692:
690:
687:
683:
679:
672:
667:
665:
660:
658:
653:
652:
649:
642:
638:
635:
634:
621:
617:
612:
607:
602:
597:
593:
589:
585:
578:
570:
566:
562:
558:
551:
543:
539:
535:
531:
527:
523:
516:
508:
504:
500:
496:
492:
488:
481:
473:
469:
464:
459:
454:
449:
445:
441:
437:
430:
422:
418:
413:
408:
403:
398:
394:
390:
386:
379:
371:
367:
363:
357:
349:
345:
341:
337:
330:
322:
318:
312:
308:
298:
295:
294:
288:
286:
275:
273:
269:
265:
255:
253:
249:
245:
241:
236:
234:
230:
229:glycosylation
226:
222:
216:
214:
210:
206:
205:antimicrobial
202:
197:
193:
189:
185:
181:
177:
167:
164:
160:
156:
152:
148:
144:
140:
136:
132:
128:
120:
112:
100:
97:
93:
90:
87:
83:
78:
74:
71:
68:
66:
62:
58:
54:
50:
49:Gallus gallus
46:
42:
37:
30:
25:
20:
1133:
742:Antithrombin
591:
587:
577:
560:
556:
550:
525:
521:
515:
490:
486:
480:
446:(11): 1543.
443:
440:Biomedicines
439:
429:
392:
388:
378:
370:the original
366:steadyhealth
365:
362:"Conalbumin"
356:
339:
335:
329:
320:
311:
281:
261:
237:
225:carbohydrate
217:
180:binding site
173:
135:glycoprotein
130:
126:
125:
33:PDB 1gvc EBI
1101:Parvalbumin
1091:Lactalbumin
983:Lactoferrin
934:Fibronectin
891:Plasminogen
871:Angiostatin
852:Transferrin
812:Haptoglobin
801:Orosomucoid
769:Transcortin
594:: 6504518.
297:Egg allergy
268:lactoferrin
264:lactoferrin
159:transferrin
151:amino acids
89:Swiss-model
39:Identifiers
1153:Categories
1070:Prealbumin
1032:Conalbumin
637:Conalbumin
303:References
240:asparagine
131:conalbumin
114:Asparagine
85:Structures
80:Search for
1037:Ovalbumin
1024:Egg white
896:Properdin
876:Hemopexin
806:alpha-2 (
799:alpha-1 (
774:alpha-2 (
767:alpha-1 (
689:globulins
389:Nutrients
252:asparagus
188:disulfide
170:Structure
155:ovalbumin
1134:see also
1015:Albumins
886:Factor H
620:28386310
542:19886663
507:29502401
472:34829772
421:26556366
291:See also
248:nitrogen
221:homology
213:bacteria
143:proteins
99:InterPro
44:Organism
958:Edestin
732:alpha-2
718:alpha-1
708:serpins
611:5366766
463:8615417
412:4663581
201:embryos
147:daltons
133:) is a
95:Domains
65:UniProt
1042:Avidin
936:(fFN:
863:other:
792:other:
643:(MeSH)
618:
608:
540:
505:
470:
460:
419:
409:
244:glycan
176:folded
70:P02789
56:Symbol
1106:Ricin
1079:Other
927:Other
686:Serum
616:PMID
592:2017
538:PMID
503:PMID
468:PMID
417:PMID
209:iron
161:and
606:PMC
596:doi
565:doi
530:doi
495:doi
458:PMC
448:doi
407:PMC
397:doi
344:doi
137:of
1155::
810:,
724:,
614:.
604:.
590:.
586:.
561:57
559:.
536:.
526:57
524:.
501:.
491:66
489:.
466:.
456:.
442:.
438:.
415:.
405:.
391:.
387:.
364:.
340:46
338:.
319:.
287:.
1097:)
1093:(
946:/
940:)
839::
814:)
803:)
778:)
771:)
760::
748:)
744:(
738:)
734:(
728:)
720:(
710::
670:e
663:t
656:v
622:.
598::
571:.
567::
544:.
532::
509:.
497::
474:.
450::
444:9
423:.
399::
393:7
350:.
346::
323:.
129:(
59:?
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