Results 141 to 150 of about 55,976 (202)
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Science, 1992
Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune . This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa
M, Potts +3 more
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Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune . This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa
M, Potts +3 more
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Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1978
Abstract In previous studies, particularly of primates, a high degree of concordance was obtained between an evolutionary pattern based on comparative anatomy and another based on a reconstruction of the possible pathway of evolution of the myoglobin molecule.
A E, Romero-Herrera +3 more
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Abstract In previous studies, particularly of primates, a high degree of concordance was obtained between an evolutionary pattern based on comparative anatomy and another based on a reconstruction of the possible pathway of evolution of the myoglobin molecule.
A E, Romero-Herrera +3 more
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Cellular and Molecular Life Sciences, 1998
The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the ...
T, Suzuki, K, Imai
exaly +3 more sources
The distribution, physiological function, amino acid sequence and gene structure of myoglobin and myoglobin-like proteins from various taxa are summarized, and their evolution is discussed. Although it has long been thought that all haemoglobins and myoglobins have evolved from a common ancestral gene, the knowledge presently accumulated about the ...
T, Suzuki, K, Imai
exaly +3 more sources
Acta Physiologica Scandinavica, 1955
Summary.Incorporation of radioiron into myoglobin of the muscles of guinea‐pigs and rats was found to be depressed to a similar extent as into hemoglobin under the effect of exposure to a dose of (500–1,400 r of) roentgen rays, in contrast to hemins, the formation of which is not in close connection with mitotic processes as that of cytochrom b or ...
R, BONNICHSEN, G, HEVESY, A, AKESON
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Summary.Incorporation of radioiron into myoglobin of the muscles of guinea‐pigs and rats was found to be depressed to a similar extent as into hemoglobin under the effect of exposure to a dose of (500–1,400 r of) roentgen rays, in contrast to hemins, the formation of which is not in close connection with mitotic processes as that of cytochrom b or ...
R, BONNICHSEN, G, HEVESY, A, AKESON
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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
A, ROSSIFANELLI, E, ANTONINI, A, CAPUTO
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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
A, ROSSIFANELLI, E, ANTONINI, A, CAPUTO
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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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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 ...
P, Eisenberger, P S, Pershan
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