myoglobin


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myoglobin

 [mi´o-glo″bin]
the oxygen-transporting pigment of muscle, a type of hemoprotein resembling a single subunit of hemoglobin, being composed of one globin polypeptide chain and one heme group.

my·o·glo·bin (Mb, MbCO, MbO2),

(mī'ō-glō'bin), [MIM*160000]
The oxygen-carrying and storage protein of muscle, resembling hemoglobin but containing only one subunit and one heme as part of the molecule (rather than the four of hemoglobin), and with a molecular weight approximately one quarter that of hemoglobin.
[myo- + hemoglobin]

myoglobin

/myo·glo·bin/ (mi″o-glo´bin) the oxygen-transporting pigment of muscle, a hemoprotein that resembles a single subunit of hemoglobin, being composed of one globin polypeptide chain and one heme group.

myoglobin

(mī′ə-glō′bĭn)
n.
A single-chain, iron-containing protein found in muscle fibers, structurally similar to a single subunit of hemoglobin and having a higher affinity for oxygen than hemoglobin of the blood.

myoglobin

[mī′ōglō′bin]
Etymology: Gk, mys + L, globus, ball
a ferrous globin complex in muscle consisting of one heme molecule containing one iron molecule attached to a single globin chain. Myoglobin is responsible for the red color of muscle and for its ability to store oxygen. Normal blood levels of myoglobin are 0-85 ng/mL. Excessive myoglobin levels may result from burns, muscle-wasting diseases, acute myocardial infarction, or trauma.

my·o·glo·bin

(mī'ō-glō'bin)
The oxygen-transporting and storage protein of muscle, resembling blood hemoglobin in function but with a molecular weight approximately one quarter that of hemoglobin. Serum levels of this protein are often measured to facilitate diagnosis of an acute myocardial infarction; it is released into the circulation within 2-4 hours after myocardial infarction, peaks at about 8-12 hours, and returns to normal after 18-24 hours.
See also: oxymyoglobin
Synonym(s): muscle hemoglobin.

myoglobin

The muscle cell equivalent of the haemoglobin of the blood. Myoglobin acts as a temporary oxygen store from which oxygen is drawn as the muscle requires it.

myoglobin

a relatively small globular protein (MW = 17 000) consisting of 153 amino acids in a POLYPEPTIDE CHAIN and one HAEM group. The molecule is found in the muscles of vertebrates and some invertebrates (giving the muscles a red colour) and has a high affinity for oxygen.

Myoglobin

A protein that holds oxygen in heart and skeletal muscle. It rises after damage to either of these muscle types.
Mentioned in: Myoglobin Test

myoglobin (mīˑ·ō·glōˈ·bin),

n oxygen- and iron-carrying compound in muscles.

myoglobin

the oxygen-transporting pigment of muscle, a conjugated protein resembling a single subunit of hemoglobin, being composed of one globin polypeptide chain and one heme group.
References in periodicals archive ?
Proteins tend to stick together at high concentrations, impairing their function, so it was unclear how myoglobin was able to help the body store enough oxygen to allow mammals, such as whales and seals, to endure underwater for long periods of time without breathing.
4 Effect of nickel oxide nanoparticles on the electron transfer of myoglobin to the electrode surface, and vice versa:
Diving animals have higher concentrations of hemoglobin and myoglobin in their bodies than humans do, so these animals can store more oxygen.
The most striking laboratory findings concerning this patient are the extremely elevated blood glucose with acidosis and concomitant increases in CK and myoglobin.
In this study, using pork meat showing actual signs of PSE, we compared the amounts of myoglobin and other meat properties between genetically normal PSE meat and sRyR1-heterozygous PSE meat.
We therefore surmise that if alkalinising the urine does in fact reduce the rate of precipitation of myoglobin in the renal tubules, acetazolamide may be used effectively in this clinical scenario.
They discovered myoglobin, a common protein, in the brain and liver of the carp, while the protein is only usually found in the heart and muscle cells of humans and vertebrate animals.
With the muscular injury of rhabdomyolysis, serum CK levels rise, as do serum myoglobin, aldolase, aminotransferases and lactate dehydrogenase (LDH).
Laboratory tests showed increases in (normal values are shown in parentheses) C-reactive protein (CRP) 40 mg/L (<9), creatine kinase (CK) 224 U/L (<170), lactate dehydrogenase (LDH) 244 U/L (<240), and myoglobin 416 ng/mL (<90).
In addition, myoglobin is a small, bright red protein.
has edited the latest edition, which contains seven articles on the following topics: solid-state and solution routes to manipulating hexanuclear transition metal chalcohalide clusters; doped semiconductor nanocrystals; stereochemical aspects of metal Xanthate complexes; trivalent uranium; comparison of the chemical biology of NO and HNO; the origins and consequences of alterations of nucleobase pKa values upon metal coordinatoin; and the functionalization of myoglobin.