|Ref Sequence Id||NP_803450.2|
|Amino Acid Lenth||704|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||serum, milk|
|Protein Function||Role in iron metabolism; delivers iron to cells via receptor mediated endocytosis; remove toxic free iron from blood; antibacterial;|
|Biochemical Properties||Binding of iron at terminals are pH dependant; affinity for Fe3+ decreases at lower pH; Glycan chains enhances solubility by virtue of their hydrophilic groups and increased charges;|
|Significance in milk||Resistant to gastric hydrolysis; render biological activity in gastrointestinal tract|
|PTMs||Glycosylated; carbohydrate content varies from 3 to 11.8% of total protein weight; biantennary structure; presence of branched, hetero N-glycan chains; each glycan consists of two sialic acid, two galactose, three mannose and four N-acetylglucosamine residues;|
|Bibliography||1. Britton, J. R. and Koldovský, O. (1989) Gastric luminal digestion of lactoferrin and transferrin by preterm infants. Early Hum. Dev. 19, 127–135. |
2. 1. Britton, J. R. and Koldovský, O. (1989) Gastric luminal digestion of lactoferrin and transferrin by preterm infants. Early Hum. Dev. 19, 127–135.
3. 1. MacGillivray, R. T., Mendez, E., Sinha, S. K., Sutton, M. R., Lineback-Zins, J., and Brew, K. (1982) The complete amino acid sequence of human serum transferrin. Proc. Natl. Acad. Sci. U. S. A. 79, 2504–2508.
4. 1. Kerckaert, J. P. and Bayard, B. (1982) Glycan uniformity within molecular variants of transferrin with distinct affinity for concanavalin A. Biochem. Biophys. Res. Commun. 105, 1023–1030.
5. 1. Aisen, P. and Listowsky, I. (1980) Iron transport and storage proteins. Annu. Rev. Biochem. 49, 357–393.
6. 1. Princiotto, J. V and Zapolski, E. J. (1975) Difference between the two iron-binding sites of transferrin. Nature 255, 87–88.
7. 1. Thakurta, P. G., Choudhury, D., Dasgupta, R., and Dattagupta, J. K. (2004) Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study. Biochem. Biophys. Res. Commun. 316, 1124–1131.