Results 311 to 320 of about 117,263 (356)
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1964
Publisher Summary This chapter describes hemoglobin and myoglobin. Hemoglobin and myoglobin are, among all proteins, ones that have been, and are, most actively studied; an enormous number of papers have been published over the past hundred years on all aspects of their properties and behavior. The study of these proteins has gone beyond the interest
Antonini E, Caputo A, Rossifanelli A
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Publisher Summary This chapter describes hemoglobin and myoglobin. Hemoglobin and myoglobin are, among all proteins, ones that have been, and are, most actively studied; an enormous number of papers have been published over the past hundred years on all aspects of their properties and behavior. The study of these proteins has gone beyond the interest
Antonini E, Caputo A, Rossifanelli A
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Nitrite coordination in myoglobin
Journal of Inorganic Biochemistry, 2017The coordination of nitrite in myoglobin (Mb) has been characterized by resonance Raman spectroscopy and the frequencies of the nitrite bound to the heme Fe as well to the 2-vinyl have been computed by density functional theory (DFT) calculations. The DFT Natural Bond Orbital (NBO) analysis and the extensive isotope-labeling in the resonance Raman ...
Ioannou, Androulla +7 more
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1981
Publisher Summary This chapter presents procedures for the isolation of intracellular oxygen-binding proteins of tissues, called “tissue hemoglobins” in the widest sense. All of these, except Ascaris and yeast hemoglobin, are monomers or dimers having a minimum molecular weight of 18,000 with similar optical spectra and chemical reactivity ...
Beatrice A. Wittenberg +1 more
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Publisher Summary This chapter presents procedures for the isolation of intracellular oxygen-binding proteins of tissues, called “tissue hemoglobins” in the widest sense. All of these, except Ascaris and yeast hemoglobin, are monomers or dimers having a minimum molecular weight of 18,000 with similar optical spectra and chemical reactivity ...
Beatrice A. Wittenberg +1 more
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Magnetic Resonance Studies of Met-Myoglobin and Myoglobin Azide
The Journal of Chemical Physics, 1967The variation of electron spin resonance lineshapes with orientation of single-crystal myoglobins are studied for high-spin (S=52) Fe3+ in met-myoglobin and low-spin (S=½) Fe3+ in myoglobin azide. It is found that for both these crystals random variations of about 2° in the orientation of the symmetry axes contribute significantly to the observed ...
Peter S. Pershan, P. Eisenberger
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Archives of Biochemistry and Biophysics, 1960
Abstract The myoglobin content of the skeletal muscles of the rat was found to vary between 0.7 and 1.2 mg./g. fresh muscle. The content of cytochrome c which is extractable with water was found to vary between 0.0122 and 0.0187 mg./g. fresh muscle.
G.v. Ehrenstein +3 more
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Abstract The myoglobin content of the skeletal muscles of the rat was found to vary between 0.7 and 1.2 mg./g. fresh muscle. The content of cytochrome c which is extractable with water was found to vary between 0.0122 and 0.0187 mg./g. fresh muscle.
G.v. Ehrenstein +3 more
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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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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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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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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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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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