How To Use Myoglobin In A Sentence
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Harbor seals have muscles rich in myoglobin, an oxygen carrying molecule.
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By mutations that place the histidine in a similar distance to the heme as in the active site of peroxidases, compound I of myoglobin has been observed, probably owing to an increased rate of heterolysis.
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Using this method Perutz determined the molecular structure of the protein haemoglobin that transports oxygen in the blood, and Kendrew, his colleague at Cambridge University, determined the molecular structure of the smaller, related protein myoglobin.
The Nobel Prize in Chemistry 1962 - Speed Read
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The heme of another protein, myoglobin, carries oxygen within muscle cells.
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The tertiary structure of myoglobin is that of a typical water soluble globular protein.
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The blood protein hemoglobin and its relative, myoglobin, carry and store life-giving oxygen in many animals.
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This nematode haemoglobin is chemically similar to myoglobin and has the highest affinity for oxygen of any known animal haemoglobin.
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Whale muscles contain large amounts of myoglobin, a protein that pulls oxygen from the blood.
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In addition, adult respiratory distress syndrome has been reported. 10 Cardiovascular instability with severe hypotension and metabolic acidosis may predominate due to the volume depletion, cardiac failure and arrhythmias. 13 Oliguric renal failure develops due to pre-renal azotemia, myoglobinuria and a direct toxic effect of colchicine on the renal tubules.
Colchicine Poisoning
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Further studies show that myoglobin, which is an in vivo biomolecule, is able to accelerate the scavenging of H2O2 by NADH notably due to its peroxidatic activity.
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Myositis is also called azoturia, ‘tying-up’, ‘Monday morning syndrome’, paralytic myoglobinuria and rhabdomyolysis and although the underlying causes may be different the clinical presentation is similar.
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A number of INS studies have been performed on proteins such as myoglobin, lysozyme, and [beta] lactoglobulin in which the low-frequency vibrational density of states has been measured.
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In this setting, a serum sample with normal color indicates myoglobinuria, whereas a pigmented brown or red serum sample indicates hemoglobinuria.
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With porcine myoglobin genomic DNA fragment cloned in a cosmid as probe, the chromosome location of this gene was determined by fluorescent in situ hybridization (FISH).
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This nematode haemoglobin is chemically similar to myoglobin and has the highest affinity for oxygen of any known animal haemoglobin.
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The key, she believes, may be the iron content of the blood and muscle proteins hemoglobin and myoglobin.
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In this setting, a serum sample with normal color indicates myoglobinuria, whereas a pigmented brown or red serum sample indicates hemoglobinuria.
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Both these changes occur because heat denatures the myoglobin.
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The definitive (and gruesome) proof came with the discovery of the human muscle protein myoglobin in the fossilized human feces of a prehistoric Anasazi pueblo Indian.
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The majority of iron in humans is located in the porphyrin ring of heme that is incorporated into proteins and enzymes such as myoglobin, hemoglobin, cytochromes, catalases, and peroxidases.
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The key, she believes, may be the iron content of the blood and muscle proteins hemoglobin and myoglobin.
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Contamination of the apoprotein by myoglobin was assessed spectrophotometrically.
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The tertiary structure of myoglobin is that of a typical water soluble globular protein.
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The key, she believes, may be the iron content of the blood and muscle proteins hemoglobin and myoglobin.
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Hemoglobin, myoglobin, cytochromes, and other proteins are involved in oxygen transport and utilization.
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Myoglobin is a red, oxygen - binding protein found in muscles.
