Transferrin
Mammalian protein found in Homo sapiens / From Wikipedia, the free encyclopedia
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Transferrins are glycoproteins found in vertebrates which bind and consequently mediate the transport of iron (Fe) through blood plasma.[5] They are produced in the liver and contain binding sites for two Fe3+ ions.[6] Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein.[7][8]
Transferrin | |||||||||
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Identifiers | |||||||||
Symbol | Transferrin | ||||||||
Pfam | PF00405 | ||||||||
InterPro | IPR001156 | ||||||||
PROSITE | PDOC00182 | ||||||||
SCOP2 | 1lcf / SCOPe / SUPFAM | ||||||||
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Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h). Transferrin has a molecular weight of around 80 kDa and contains two specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (association constant is 1020 M−1 at pH 7.4)[9] but decreases progressively with decreasing pH below neutrality. Transferrins are not limited to only binding to iron but also to different metal ions.[10] These glycoproteins are located in various bodily fluids of vertebrates.[11][12] Some invertebrates have proteins that act like transferrin found in the hemolymph.[11][13]
When not bound to iron, transferrin is known as "apotransferrin" (see also apoprotein).