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Myoglobin

Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of


vertebrates in general and in almost all mammals. It is related to hemoglobin,
which is the iron- and oxygen-binding protein in blood, specifically in the red
blood cells. In humans, myoglobin is only found in the bloodstream after muscle
injury. It is an abnormal finding, and can be diagnostically relevant when found in
blood.
Myoglobin is the primary oxygen-carrying pigment of muscle tissues. High
concentrations of myoglobin in muscle cells allow organisms to hold their breath
for a longer period of time. Diving mammals such as whales and seals have
muscles with particularly high abundance of myoglobin. Myoglobin is found in
Type I muscle, Type II A and Type II B, but most texts consider myoglobin not to
be found in smooth muscle.
Myoglobin was the first protein to have its three-dimensional structure revealed by
X-ray crystallography. This achievement was reported in 1958 by John Kendrew
and associates. For this discovery, John Kendrew shared the 1962 Nobel Prize in
chemistry with Max Perutz. Despite being one of the most studied proteins in
biology, its physiological function is not yet conclusively established: mice
genetically engineered to lack myoglobin are viable, but showed a 30% reduction
in volume of blood being pumped by the heart during a contraction. They adapted
to this deficiency through natural reactions to inadequate oxygen supply (hypoxia)
and a widening of blood vessels (vasodilation). In humans myoglobin is encoded
by the MB gene.

Role of Myoglobin
Meat color
Myoglobin contains hemes, pigments responsible for the color of red meat. The
color that meat takes is partly determined by the degree of oxidation of the
myoglobin. In fresh meat the iron atom is the ferrous state bound to a dioxygen
molecule (O2). Meat cooked well done is brown because the iron atom is now in
the ferric (+3) oxidation state, having lost an electron. If meat has been exposed to
nitrites, it will remain pink because the iron atom is bound to NO, nitric oxide (true

of, e.g., corned beef or cured hams). Grilled meats can also take on a pink "smoke
ring" that comes from the iron binding to a molecule of carbon monoxide. [9] Raw
meat packed in a carbon monoxide atmosphere also shows this same pink "smoke
ring" due to the same principles. Notably, the surface of this raw meat also displays
the pink color, which is usually associated in consumers' minds with fresh meat.
This artificially induced pink color can persist, reportedly up to one year.[10]
Hormel and Cargill are both reported to use this meat-packing process, and meat
treated this way has been in the consumer market since 2003.
Role in disease
Myoglobin is released from damaged muscle tissue (rhabdomyolysis), which has
very high concentrations of myoglobin. The released myoglobin is filtered by the
kidneys but is toxic to the renal tubular epithelium and so may cause acute renal
failure. It is not the myoglobin itself that is toxic (it is a protoxin) but the
ferrihemate portion that is dissociated from myoglobin in acidic environments
(e.g., acidic urine, lysosomes).
Myoglobin is a sensitive marker for muscle injury, making it a potential marker for
heart attack in patients with chest pain.[13] However, elevated myoglobin has low
specificity for acute myocardial infarction (AMI) and thus CK-MB, cTnT, ECG,
and clinical signs should be taken into account to make the diagnosis.

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