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Transferrin (mg/dL) = 0.8 x TIBC (μg of iron/dL) – 43; 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 ...
Transferrin also has a transferrin iron-bound receptor; it is a disulfide-linked homodimer. [16] In humans, each monomer consists of 760 amino acids. It enables ligand bonding to the transferrin, as each monomer can bind to one or two atoms of iron. Each monomer consists of three domains: the protease, the helical, and the apical domains.
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.
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.
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]
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.
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.
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]