Examples of myoglobin in the following topics:
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- Heart muscle also contains large amounts of a pigment called myoglobin.
- Myoglobin is similar to hemoglobin in that it contains a heme group (an oxygen binding site).
- Myoglobin transfers oxygen from the blood to the muscle cell and stores reserve oxygen for aerobic metabolic function in the muscle cell.
- The heme component of myoglobin, shown in orange, binds oxygen.
- Myoglobin provides a back-up store of oxygen to muscle cells.
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- Due to their large oxygen requirements, slow-twitch fibers are associated with large numbers of blood vessels, mitochondria, and
high concentrations of myoglobin, an oxygen-binding protein
found in the blood that gives muscles their reddish color.
- As fast-twitch fibers generally do not require oxygenation, they contain fewer blood vessels and mitochondria than slow-twitch fibers and less
myoglobin, resulting in a paler colour.
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- Type I fibers appear red due to the presence of the oxygen-binding protein myoglobin.
- They contain large and numerous mitochondria with high levels of myoglobin that gives them a red pigmentation.
- Type II fibers are white due to the absence of myoglobin and a reliance on glycolytic enzymes.
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- Additionally, myoglobin and mitochondrial cytochrome oxidase are thought to be adversely affected.
- For example, carbon monoxide binds to the hemeprotein myoglobin and impairs its ability to utilize oxygen.
- This results following a recurrence of increased carboxyhemoglobin levels and this effect may be due to a late release of carbon monoxide from myoglobin, which subsequently binds to hemoglobin.
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- With aging, levels of ATP, CTP, and myoglobin begin to decline, reducing the muscle's ability to function.
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- Cardiac muscle and skeletal muscle both contain the protein myoglobin, which stores oxygen.