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Transferrin

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transferrin [′tranz′fer·ən]
(biochemistry)
Any of various beta globulins in blood serum which bind and transport iron to the bone marrow and storage areas.

Transferrin 

(also siderophilin), any of a group of related complex proteins (glycoproteins) that transport Fe3+ iron ions in organisms. The carbohydrate component of transferrins constitutes approximately 5.5 percent. The molecular weight is approximately 80,000.

Transferrins occur in blood plasma, milk, and egg albumin (conalbumin). In blood plasma, their main functions are the transport of iron (with one molecule of transferrin binding two atoms of trivalent iron) to the reticulocytes, where hemoglobin is synthesized, and the maintenance of the Fe2+/Fe3+ ratio at a certain level. Upon electrophoresis of plasma proteins, transferrin is found in the β-globulin fraction. Transferrins are found in various genetically dependent forms, which have similar physical and chemical properties. A deficiency of transferrin in organisms leads to a number of pathological states caused by disruption of iron metabolism.

REFERENCE

Glikoproteiny, vol. 2. Moscow, 1969. (Translated from English.)


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CP is vitally important in regulating the ionic state of iron in particular, oxidizing Fe2 + to Fe3 + and thus permitting incorporation of the iron into transferrin without the formation of toxic iron products.
[ILLUSTRATION OMITTED] Transferrin is a glycoprotein (a molecule made of amino acids and sugar groups) produced in liver cells.
CellPrime rTransferrin AF is the first animal-free alternative to serum-derived human or bovine transferrin for industrial cell culture and upstream biopharmaceutical applications.
 
 
 
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