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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]
Iron tests are groups of clinical chemistry laboratory blood tests that are used to evaluate body iron stores or the iron level in blood serum. Other terms used for the same tests are iron panel , iron profile , iron indices , iron status or iron studies .
Transferrin saturation (TS), measured as a percentage, is a medical laboratory value. It is the value of serum iron divided by the total iron-binding capacity [1] of the available transferrin, the main protein that binds iron in the blood, this value tells a clinician how much serum iron is bound. For instance, a value of 15% means that 15% of ...
Serum iron is a medical laboratory test that measures the amount of circulating iron that is bound to transferrin and freely circulate in the blood. Clinicians order this laboratory test when they are concerned about iron deficiency, which can cause anemia and other problems. 65% of the iron in the body is bound up in hemoglobin molecules in red blood cells.
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.
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Ferritin genes are highly conserved between species. All vertebrate ferritin genes have three introns and four exons. [8] In human ferritin, introns are present between amino acid residues 14 and 15, 34 and 35, and 82 and 83; in addition, there are one to two hundred untranslated bases at either end of the combined exons. [9]