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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. 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

  5. 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 ...

  6. Max Perutz - Wikipedia

    en.wikipedia.org/wiki/Max_Perutz

    Max Ferdinand Perutz OM CH CBE FRS (19 May 1914 – 6 February 2002) [3] was an Austrian-born British molecular biologist, who shared the 1962 Nobel Prize for Chemistry with John Kendrew, for their studies of the structures of haemoglobin and myoglobin.

  7. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    A representation of the structure of myoglobin, showing alpha helices, represented by ribbons.This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and John Kendrew in 1958, for which they received a Nobel Prize in Chemistry

  8. 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.

  9. Exertional rhabdomyolysis - Wikipedia

    en.wikipedia.org/wiki/Exertional_rhabdomyolysis

    Exertional rhabdomyolysis, the exercise-induced muscle breakdown that results in muscle pain/soreness, is commonly diagnosed using the urine myoglobin test accompanied by high levels of creatine kinase (CK). Myoglobin is the protein released into the bloodstream when skeletal muscle is broken down. The urine test simply examines whether ...