Transferrin

Transferrin is a protein that plays an important role in transporting iron in the body. It is one of the main proteins in blood plasma and is found in red blood cells, liver and other tissues.

Transferrin consists of four polypeptide chains that are linked by disulfide bridges. Each chain contains two cysteine ​​residues that form disulfide bonds. This ensures the stability of the transferrin molecule and its ability to bind to iron ions.

In the blood, transferrin performs several functions. It binds iron that is ingested or synthesized in the body and transports it to tissues, where it is used to form hemoglobin in red blood cells and myoglobin in muscles. Transferrin is also involved in the regulation of iron levels in the blood, as it can take up iron from the plasma and transport it to the liver, where it is stored.

In addition, transferrin plays an important role in immune processes. It is involved in the formation of antibodies and other defense mechanisms of the body.

Thus, transferrin is an important blood plasma protein that is involved in the transport of iron and the regulation of its level in the body.

Transferrin is the main protein portion of the iron-binding protein heme complex. ***Transferrin*** is a blood plasma glycoprotein that performs the function of transferring iron (ferritin) associated with other proteins and trace elements in the body. It is considered the main iron complex in human serum.

The name transferrin is related to its name in chemical element nomenclature, which is derived from the Latin term "ferrum", meaning iron, and the Greek suffix "philia", meaning affinity. This means that the transferrin molecule is primarily used to transport iron ions.

Transferrin is a heterogeneous glycoprotein that consists of a polypeptide chain and a carbohydrate chain. The polypeptide chain makes up about 78% of the total transferrin, and the carbohydrate chain (glycosylation) makes up about 22%.

Transported low molecular weight metals such as Na+, K+, Mg2+, Cu2+, Mn2+, Cd2+ and Ca2+; d-serine. Reduces the oxidative function of vitamin C.

Hemopexins and other proteins (and