Myoglobin antibody

Background of Myoglobin antibody

Myoglobin (Mygb) is a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal muscle fibers and functions as facilitator of oxygen transport, storage of oxygen and a scavenger of nitric oxide or reactive oxygen species. Mygb and hemoglobin are the iron containing proteins that carry oxygen in the body. The heme group present in neuroglobin, Mygb, Hemoglobin, cytochrome b and many other heme containing proteins consist of a complex protoporphyrin ring bound with iron in the ferrous state. Myoglobin measurement is used in many clinical diagnoses and has become an important tool in prognosis and diagnosis of several diseases. Mygb is (M(r) 18,000) and fatty acid-binding protein (M(r) 15,000), are low molecular mass cytoplasmic proteins that are considered useful biochemical markers for early detection or exclusion of acute myocardial infarction, and also for early estimation of infarct size. As each of these proteins shows renal clearance, the influence of renal function on the estimation of infarct size from their plasma concentration curves can be drawn (1). Myoglobin plasma levels correlates with muscle wasting in patients with cancer-related cachexia. Myoglobin expression is increased in muscles in the presence of testosterone by aerobic exercises (1).
Hemoglobin and Mygb are among the most extensively studied proteins along with nitrite one of the most studied signal transducing small molecules. During the last decade, multiple physiological studies have surprisingly revealed that nitrite represents a biological reservoir of NO by R-type catalysis in the oxygen carrying process of hemoglobin and Mygb that can regulate hypoxic vasodilation, cellular respiration, and signaling (2). Carbon monoxide poisoning let to elevated levels of CO in blood, but its diffusion to other tissue and the tissue contents are difficult to measure and asses. Multi-compartment models for CO diffusion to muscle and other sub-compartments can be achieved by measuring CO contents in Myoglobin (3). Myoglobin is protoporphyrin containing iron-binding glycoprotein with an approximate molecular weight of 19kDa (154 amino acids). The protein has a porpyrin binding domains housing one Fe(3+) ion.