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LOINC. 2500-7, 14800-7, 35215-3. Total iron-binding capacity (TIBC) or sometimes transferrin iron-binding capacity is a medical laboratory test that measures the blood's capacity to bind iron with transferrin. [1] Transferrin can bind two atoms of ferric iron (Fe 3+) with high affinity. It means that transferrin has the capacity to transport ...
Export occurs through ferroportin, often aided by hephaestin (Hp) and/or ceruloplasmin (Cp), and repressed by hepcidin. 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.
The recommended daily intake of iron for both men and women is 8 mg, with an upper limit of 45 mg/day. According to the World Health Organization, hemoglobin levels below 12 g/dl in women and 13 mg/dl in men indicate anemia. [173] The NHANES III survey found that anemia affects 10.2% of women and 11% of men over 65, with prevalence increasing ...
Iron deficiency, or sideropenia, is the state in which a body lacks enough iron to supply its needs. Iron is present in all cells in the human body and has several vital functions, such as carrying oxygen to the tissues from the lungs as a key component of the hemoglobin protein, acting as a transport medium for electrons within the cells in the form of cytochromes, and facilitating oxygen ...
Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals. It is the primary intracellular iron-storage protein in both prokaryotes and eukaryotes, keeping iron in a soluble and non ...
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.
Structure. In humans, transferrin consists of a polypeptide chain containing 679 amino acids and two carbohydrate chains. The protein is composed of alpha helices and beta sheets that form two domains. [18] The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site.
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 ...