Myoglobin
Description
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.
Product Specs
The starting material, obtained from the donor, has undergone rigorous testing and is certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.
Product Science Overview
Myoglobin is structurally similar to hemoglobin, the oxygen-binding protein found in red blood cells. Both proteins contain a heme group, which is responsible for their ability to bind oxygen. The heme group contains an iron atom that can reversibly bind to an oxygen molecule. This binding imparts a red-brown color to the protein, contributing to the characteristic color of muscle tissue .
Unlike hemoglobin, which has a quaternary structure consisting of four subunits, myoglobin is a monomeric protein. This means it consists of a single polypeptide chain. Myoglobin’s primary function is to store oxygen and facilitate its transport from the cell membrane to the mitochondria, where it is used for aerobic respiration .
Myoglobin was the first protein to have its three-dimensional structure determined by X-ray crystallography. This groundbreaking work was conducted by John Kendrew, who received a share of the Nobel Prize in Chemistry in 1962 for his contributions. The elucidation of myoglobin’s structure provided significant insights into protein folding and function, marking a milestone in the field of structural biology .
In humans, myoglobin is found in high concentrations in the heart and skeletal muscles. It is particularly abundant in Type I (slow-twitch) muscle fibers, which are adapted for endurance activities and rely heavily on aerobic metabolism. Myoglobin’s ability to bind and release oxygen efficiently makes it essential for maintaining oxygen supply during sustained muscle activity .
Myoglobin also plays a critical role in diving mammals, such as whales and seals, which have high concentrations of myoglobin in their muscles. This adaptation allows them to store large amounts of oxygen and remain submerged for extended periods .
Myoglobin is released into the bloodstream following muscle injury, such as in cases of myocardial infarction (heart attack) or rhabdomyolysis (severe muscle breakdown). Elevated levels of myoglobin in the blood can be detected through laboratory tests and are used as a diagnostic marker for these conditions .
However, excessive myoglobin in the bloodstream can be harmful, as it can lead to kidney damage. This condition, known as myoglobinuria, occurs when myoglobin is filtered by the kidneys and precipitates in the renal tubules, causing obstruction and renal failure .
