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Transferrin (mg/dL) = 0.7 x TIBC (μg of iron/dL) To measure TIBC in the blood is less expensive than a direct measurement of transferrin. [4] [5] The TIBC should not be confused with the unsaturated iron-binding capacity or UIBC (LOINC 2501-5, 22753-8 & 35216-1). The UIBC is calculated by subtracting the serum iron from the TIBC. [6]
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.
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 .
This article, however, seems to be falsely defining TIBC as the free Fe-binding spots (which would in fact be be the UIBC = unsaturated iron-binding capacity). For example, the article states the following, "Generally speaking, if the iron stores in the body are low, fewer of these spots on the transferrin molecules will be filled by iron, and ...
The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. [12] 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 ...
Human iron metabolism is the set of chemical reactions that maintain human homeostasis of iron at the systemic and cellular level. Iron is both necessary to the body and potentially toxic. Controlling iron levels in the body is a critically important part of many aspects of human health and disease.
Iron-binding proteins are carrier proteins and metalloproteins that are important in iron metabolism [1] and the immune response. [2] [3] Iron is required for life.Iron-dependent enzymes catalyze a variety of biochemical reactions and can be divided into three broad classes depending on the structure of their active site: non-heme mono-iron, non-heme diiron , or heme centers. [4]
In addition to "iron withdrawal" tactics, mammals produce an iron –siderophore binding protein, siderochelin. Siderochelin is a member of the lipocalin family of proteins, which while diverse in sequence, displays a highly conserved structural fold, an 8-stranded antiparallel β-barrel that forms a binding site with several adjacent β-strands.