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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.
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. Thus, iron toxicity from ingestion is usually the result of extraordinary circumstances like iron tablet over-consumption [42] rather than variations in diet. The type of ...
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 ...
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.
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]
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.
MerckMedicus: total iron-binding capacity (TIBC)a measure of the total amount of iron that can be bound by the transferrin in a serum sample, determined by saturating the transferrin with iron, then removing the unbound iron with an absorbent and measuring the iron in the filtrate; used in the evaluation of patients with iron deficiency or ...