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  2. Myoglobin - Wikipedia

    en.wikipedia.org/wiki/Myoglobin

    Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. It harbors only one globulin group, whereas hemoglobin has four. Although its heme group is identical to those in Hb, Mb has a higher affinity for oxygen than does hemoglobin but fewer total oxygen-storage capacities. [22]

  3. Globin - Wikipedia

    en.wikipedia.org/wiki/Globin

    Myoglobin (Mb) Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in neuroprotection from damage due to hypoxia or ischemia. [11] Neuroglobin belongs to a branch of the globin family that diverged early in evolution. Cytoglobin: an oxygen sensor expressed in multiple tissues. Related to ...

  4. Cardiac marker - Wikipedia

    en.wikipedia.org/wiki/Cardiac_marker

    Myoglobin (Mb) low specificity for myocardial infarction: 2 hours Myoglobin is used less than the other markers. Myoglobin is the primary oxygen-carrying pigment of muscle tissue. It is high when muscle tissue is damaged but it lacks specificity. It has the advantage of responding very rapidly, [10] rising and falling earlier than CK-MB or ...

  5. Heme B - Wikipedia

    en.wikipedia.org/wiki/Heme_B

    Heme B or haem B (also known as protoheme IX) is the most abundant heme. [1] Hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B.

  6. Apomyoglobin - Wikipedia

    en.wikipedia.org/wiki/Apomyoglobin

    Apomyoglobin is a type of myoglobin that does not have a haem group. [3] This means that apomyoglobin lacks the haem groups that would have their iron atoms bind to Oxygen. [4] There is a possibility, however, that apomyoglobin can bind to other different cofactors that is not a haem group. [5]

  7. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    Hemoglobin and myoglobin are examples of hemeproteins that respectively transport and store of oxygen in mammals and in some fish. [9] Hemoglobin is a quaternary protein that occurs in the red blood cell, whereas, myoglobin is a tertiary protein found in the muscle cells of mammals. Although they might differ in location and size, their ...

  8. Myoglobinuria - Wikipedia

    en.wikipedia.org/wiki/Myoglobinuria

    Under ideal situations myoglobin will be filtered and excreted with the urine, but if too much myoglobin is released into the circulation or in case of kidney problems, it can occlude the kidneys' filtration system leading to acute tubular necrosis and acute kidney injury. Other causes of myoglobinuria include: McArdle's disease

  9. Rhabdomyolysis - Wikipedia

    en.wikipedia.org/wiki/Rhabdomyolysis

    Rhabdomyolysis may cause kidney failure by several mechanisms. The most important is the accumulation of myoglobin in the kidney tubules. [10] [11] [13] Normally, the blood protein haptoglobin binds circulating myoglobin and other heme-containing substances, but in rhabdomyolysis the quantity of myoglobin exceeds the binding capacity of ...