  transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. human transferrin is encoded by the tf gene. transferrin glycoproteins bind iron very tightly, but reversibly. although iron bound to transferrin is less than 0.1% (4&nbsp;mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25&nbsp;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 (1023 mâ1 at ph 7.4) but decreases progressively with decreasing ph below neutrality. when not bound to iron, it is known as "apotransferrin" (see also apoprotein). == transport mechanism == when a transferrin protein loaded with iron encounters a transferrin receptor on the surface of a cell (e.g., to erythroid precursors in the bone marrow), it binds to it and, as a consequence, is transported into the cell in a vesicle by receptor-mediated endocytosis. the ph of the vesicle is reduced by hydrogen ion pumps ( atpases) to about 5.5, causing transferrin to release its iron ions. the receptor (with its ligand, transferrin, bound) is then transported through the endocytic cycle back to the cell surface, ready for another round of iron uptake. each transferrin molecule has the ability to carry two iron ions in the ferric form (). the gene coding for transferrin in humans is located in chromosome band 3q21. medical professionals may check serum tran
Chemical_pathology Human_proteins Iron_metabolism