Results 261 to 270 of about 67,066 (301)
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Formation and Radiosensitivity of Myoglobin
Nature, 1955HAEMOGLOBIN is laid down in the maturing erythropoietic marrow cells. Exposure to ionizing radiation depresses the formation of new erythropoietic marrow cells and may destroy any such cells already present. Anaemia resulting from this interference manifests itself after the lapse of some days in a reduced erythrocyte count and reduced haemoglobin ...
R. Bonnichsen, G. Hevesy, Åke Åkeson
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The hydration shell of myoglobin
European Biophysics Journal, 1992The space in the unit cell of a metmyoglobin crystal not occupied by myoglobin atoms was filled with water using Monte Carlo calculations. Independent calculations with different amounts of water have been performed. Structure factors were calculated using the water coordinates thus obtained and the known coordinates of the myoglobin atoms.
E. Clementi +4 more
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Structural Dynamics of Myoglobin
2008Protein structure is endowed with a complex dynamic nature, which rules function and controls activity. The experimental investigations that yield information on protein dynamics are carried out in solution; however, in most cases, the determination of protein structure is carried out by crystallography that relies on the diffraction properties of a ...
BRUNORI, Maurizio +2 more
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On the microheterogeneity of horse myoglobin
Archives of Biochemistry and Biophysics, 1960Abstract A procedure for isolating three homogeneous myoglobins, Mb I, Mb II 1 , and Mb II 2 , from horse muscle is described. The iron and sulfur content were the same in all three myoglobins and no significant difference was found in the amino acid composition.
Åke Åkeson, Hugo Theorell
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Serum Myoglobin in Rhabdomyolysis
JAMA: The Journal of the American Medical Association, 1982To the Editor.— Recently, Porter et al (1981;245:1545) reported two cases of rhabdomyolysis in patients withStreptococcusand picornavirus infection. The observations of the authors are of importance because they add these infectious agents to the already long list of viruses and bacteria involved in the pathogenesis of atraumatic rhabdomyolysis and ...
Helmut F. Kaiser +3 more
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Myoglobin chemistry and meat color.
Annual Review of Food Science and Technology, 2013Consumers rely heavily on fresh meat color as an indicator of wholesomeness at the point of sale, whereas cooked color is exploited as an indicator of doneness at the point of consumption. Deviations from the bright cherry-red color of fresh meat lead to
S. Suman, P. Joseph
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2003
Myoglobin represents the stores of oxygen in muscle tissues. Because of its relatively small mol wt, myoglobin is often used in electrophoretic techniques as a mol wt marker, and also as a test for separation efficiency in capillary electrophoresis (CE).
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Myoglobin represents the stores of oxygen in muscle tissues. Because of its relatively small mol wt, myoglobin is often used in electrophoretic techniques as a mol wt marker, and also as a test for separation efficiency in capillary electrophoresis (CE).
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ChemInform Abstract: Nitric Oxide and Myoglobins
ChemInform, 2002AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Møller, J. K. S., Skibsted, L. H.
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Crystallization of Whale Myoglobin
Nature, 1948ALTHOUGH the spectroscopic differences between blood and muscle haemoglobin were first observed by Morner1 in 1897, it was not until 1932 that Theorell2 succeeded in crystallizing myoglobin from horse-heart muscle.
Joan Keilin, K. Schmid
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Dynamics of ligand binding to myoglobin.
Biochemistry, 1975Myoglobin rebinding of carbon monoxide and dioxygen after photodissociation has been observed in the temperature range between 40 and 350 K. A system was constructed that records the change in optical absorption at 436 nm smoothly and without break ...
R. Austin +4 more
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