Myoglobin Antibody

Myoglobin (MB) also known as PVALB, is a single-chain globular protein of 153 or 154 amino acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which the remaining apoprotein folds. Two structural variants of myoglobin were described by Boyer et al. (1963) . Boulton et al. (1969) studied postmortem muscle from 2,500 people. Two Myoglobin variants were found, and in one of these substitution of lysine for glutamic acid at residue 53 was demonstrated. MG was the first protein to have its three-dimensional structure revealed. Jeffreys et al. (1984) used DNA probes isolated from the cloned gene to map the gene in human-rodent somatic cell hybrids. The locus mapped to chromosome 22q11-q13. MG is released from damaged muscle tissue (rhabdomyolysis), which has very high concentrations. The released MG is filtered by the kidneys but is toxic to the renal tubular epithelium and so may causeacute renal failure.