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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5A presents several examples of TRF length of genomic DNA from colorectal tissues of either tumor (T) or non-tumor (NT) tissue.
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The TRF group watched the same videotaped lesson but applied an alternative framework.
There are some higher-molecular-weight bands in addition to the main telomeric smear present in both the coral and Symbiodinium TRF analyses; these could either represent higher-molecular-weight modes in the telomeres or simply be the result of incomplete digestion of DNA.
The TRF consists of 113 problem items, such as difficulty following directions, disturbing other pupils, and disrupting class discipline.
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