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myoglobin

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myoglobin
myoglobin Biochem. (maɪəˈgləʊbɪn) [a. G. myoglobin (H. Günther 1921, in Virchows Arch. f. path. Anat. und Physiol. CCXXX. 150), f. myo- myo- + globin globin.] A red protein responsible for the transport of oxygen in muscle cells, which differs from hæmoglobin in containing only one hæm group and one... Oxford English Dictionary
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Myoglobin
of myoglobin. Myoglobin contains 153 amino acids. Myoglobin contains a porphyrin ring with an iron at its center. wikipedia.org
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Myoglobin Mediates Autophagy of NRK-52E in Rat Renal Tubular Epithelial ...
Myoglobin acted on NRK-52E, caused differential expressions of Pink1, Parkin, and Beclin 1, increased apoptosis, and decreased cell viability. myoglobin increased the levels of Pink1, Beclin 1 and ATG5, decreased the levels of P62 and Parkin. The level of LC3II/LC3I showed significant elevation in NRK-52E cells at after incubated with 100 μmol ...
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Myoglobin Mediates Autophagy of NRK-52E in Rat Renal Tubular ... - PubMed
RESULTS Myoglobin acted on NRK-52E, caused differential expressions of Pink1, Parkin, and Beclin 1, increased apoptosis, and decreased cell viability. myoglobin increased the levels of Pink1, Beclin 1 and ATG5, decreased the levels of P62 and Parkin. The level of LC3II/LC3I showed significant elevation in NRK-52E cells at after incubated with ...
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oxymyoglobin
oxymyoglobin Biochem. (ˌɒksɪmaɪəˈgləʊbɪn) [f. oxy- 2 + myoglobin.] The oxygenated form of myoglobin.1935 Physiol. Abstr. XIX. 578 The dissociation curve of oxymyoglobin is a hyperbola. 1953 Fruton & Simmonds Gen. Biochem. vi. 167 At a given oxygen pressure oxymyoglobin is less dissociated than oxyhe... Oxford English Dictionary
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Myoglobinuria
Myoglobin is present in muscle cells as a reserve of oxygen. 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 wikipedia.org
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Myoglobin in meat When looking at the reason why some meat is white and the rest is red, I found out it is down to the levels of myoglobin as higher levels of myoglobin are found in "slow twitch" muscles. I have also...
Myoglobin is a protein made in muscle cells. It is similar to hemoglobin, a protein made by blood cells. The color in both blood and uncooked or rare meat is due to the heme group in hemoglobin and myoglobin respectively.
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Leghemoglobin
Leghemoglobin has a slow oxygen dissociation rate, similar to myoglobin. Like myoglobin and hemoglobin, leghemoglobin has a high affinity for carbon monoxide. wikipedia.org
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Hemoprotein
Hemoglobin and myoglobin Hemoglobin and myoglobin are examples of hemeproteins that respectively transport and store of oxygen in mammals and in some fish Myoglobin Myoglobin is found in vertebrate muscle cells and is a water-soluble globular protein. wikipedia.org
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What causes the localization of myoglobin in turkey to regions of muscle tissue? I've read that myoglobin localization is responsible for the darker colour of leg muscles in turkeys. Why does this localization occur i...
Type I fibers took on fast glycolytic properties, whereas the Type II took on the slow oxidative features (such as higher levels of mitochondria and myoglobin
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Globin
The globin fold was thus the first protein fold discovered (myoglobin was the first protein whose structure was solved). Subfamilies Leghaemoglobin Myoglobin Erythrocruorin Hemoglobin, beta Hemoglobin, alpha Myoglobin, trematode type Globin, nematode Globin, lamprey wikipedia.org
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Coboglobin
A coboglobin is a synthetic compound, a metalloprotein chemically similar to hemoglobin or myoglobin but using the metal cobalt instead of iron (hence Just like hemoglobin and myoglobin, the coboglobins are able to reversibly bind molecular oxygen (O2) at the metal atom. wikipedia.org
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Chromatogram Detail - MilliporeSigma
HPLC Analysis of Thyroglobulin, gamma-Globulins, Ovalbumin, Myoglobin, and Poly-DL-Alanine on Zenix ® SEC-150, 30 cm x 7.8 mm I.D., 3 μm particles
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Rhabdomyolysis
The most important is the accumulation of myoglobin in the kidney tubules. Normally, the blood protein haptoglobin binds circulating myoglobin and other heme-containing substances, but in rhabdomyolysis the quantity of myoglobin wikipedia.org
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Heme B
Hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. Both hemoglobin and myoglobin have a coordination bond to an evolutionarily-conserved histidine, while nitric oxide synthase and cytochrome P450 have a wikipedia.org
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