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It means that transferrin has the capacity to transport approximately from 1.40 to 1.49 mg of iron per gram of transferrin present in the blood. [2] It is performed by drawing blood and measuring the maximum amount of iron that it can carry, which indirectly measures transferrin [3] since transferrin is the
The amino acids which bind the iron ion to the transferrin are identical for both lobes; two tyrosines, one histidine, and one aspartic acid. For the iron ion to bind, an anion is required, preferably carbonate (CO 2− 3). [18] [13] Transferrin also has a transferrin iron-bound receptor; it is a disulfide-linked homodimer. [16]
Transferrin is present in the serum at approximately 30 μM, and contains two iron-binding sites, each with an extremely high affinity for iron. Under normal conditions it is about 25–40% saturated, which means that any freely available iron in the serum will be immediately scavenged – thus preventing microbial growth.
Latent iron deficiency (LID), also called iron-deficient erythropoiesis, [1] is a medical condition in which there is evidence of iron deficiency without anemia (normal hemoglobin level). [2] It is important to assess this condition because individuals with latent iron deficiency may develop iron-deficiency anemia.
Large amounts of free iron in the circulation will cause damage to critical cells in the liver, the heart and other metabolically active organs. Iron toxicity results when the amount of circulating iron exceeds the amount of transferrin available to bind it, but the body is able to vigorously regulate its iron uptake.
Another important class of iron–sulfur proteins is the ferredoxins, which have multiple iron atoms. Transferrin does not belong to either of these classes. [5] The ability of sea mussels to maintain their grip on rocks in the ocean is facilitated by their use of organometallic iron-based bonds in their protein-rich cuticles.
Blood testing of the soluble transferrin receptor (sTfR) is used as a measure of functional iron status and the investigation of iron deficiency anemia. Ferritin, a routine investigation for anemia, is an acute-phase reactant, and may be elevated in states of inflammation, thereby falsely indicating that iron stores are adequate. [2]
It is thought that this protein functions to regulate circulating iron uptake by regulating the interaction of the transferrin receptor with transferrin. [6] The HFE gene contains 7 exons spanning 12 kb. [7] The full-length transcript represents 6 exons. [8] HFE protein is composed of 343 amino acids. There are several components, in sequence ...