MYOGLOBIN

myoglobin facilitates the oxygen use and storage in the muscles; and cytochromes transport electrons. Iron is also an integral part of enzymes in various tissues. The average 70-kg adult body contains around 4200 mg of iron ions. The majority (65%) can be found as haemoglobin or myoglobin, which is classified as the functional iron .Myoglobin consists of a monomeric protein chain containing one protoporphyrin group as the functional unit.Within myoglobin, the iron centre is coordinated by the four nitrogen groups of the porphyrin in addition to the coordination of a fifth nitrogen centre from a histidine (His) group. The functional unit containing the Fe(II) centre is called a haeme group and is a square-based pyramidal complex. During the oxygen binding mechanism, O2will enter trans to the His group to give an octahedrally coordinated iron species.

A protein-iron-porphyrin moleculesimilar to hemoglobin. The chief difference isthat myoglobin complexes one heme group permolecule, whereas hemoglobin complexes fourheme groups.

A globular protein formed of a heme group and a single polypeptide chain. It occurs in muscle tissue where it acts as an oxygen store.

Myoglobinis a heme-related, low-molecular-weight protein. It is mainly found in cardiac and skeletal muscle.

Human Myoglobin produced in Human Cardiac Tissues having a molecular mass of 17.5kDa.Myoglobin is released from recently injured myocardial cells within a few hours of Infarction. Peak levels are reached more quickly than CK-MB or Troponin complex.

Myoglobin from human heart has been used as a negative control in monitoring isoAsp formation during storage. It has also been used as an antigen in the study to identify self-antigens recognized by serum autoantibodies from unimmunized mice strains.