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Transferrin is highly specific to iron (III), and binds to it with an equilibrium constant of 10 23 M −1 at a pH of 7.4. [5] Thalassemia results in nontransferrin-bound iron being available in blood as all the transferrin becomes fully saturated. This free iron is toxic to the body since it catalyzes reactions that generate free hydroxyl ...
Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein. [7] [8] Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h).
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.
It is thought that this protein functions to regulate circulating iron uptake by regulating the interaction of the transferrin receptor with transferrin. [6] The HFE gene contains 7 exons spanning 12 kb. [7] The full-length transcript represents 6 exons. [8] HFE protein is composed of 343 amino acids. There are several components, in sequence ...
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.
But with iron overload (such as with frequent blood transfusions), the ability for transferrin to bind iron is exceeded and non-transferrin bound iron accumulated. This unbound iron is toxic due to its high propensity to induce oxygen species and is responsible for cellular damage. The prevention of iron overload protects patients from ...
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 ...
Normally, HFE facilitates the binding of transferrin, which is iron's carrier protein in the blood. Transferrin levels are typically elevated at times of iron depletion (low ferritin stimulates the release of transferrin from the liver). When transferrin is high, HFE works to increase the intestinal release of iron into the blood.