Results 301 to 310 of about 119,093 (354)
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Evolution of myoglobin

Cellular and Molecular Life Sciences CMLS, 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
openaire   +2 more sources

Formation of Myoglobin

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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Mice without myoglobin

Nature, 1998
Myoglobin, an intracellular haemoprotein expressed in the heart and oxidative skeletal myofibres of vertebrates, binds molecular oxygen and may facilitate oxygen transport from erythrocytes to mitochondria, thereby maintaining cellular respiration during periods of high physiological demand. Here we show, however, that mice without myoglobin, generated
D J, Garry   +7 more
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Life without myoglobin

Cellular and Molecular Life Sciences, 2000
Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals [1]. Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria [1-3].
D J, Garry   +3 more
openaire   +3 more sources

Magnetic Resonance Studies of Met-Myoglobin and Myoglobin Azide

The Journal of Chemical Physics, 1967
The 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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Hemoglobin and Myoglobin

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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Structural Dynamics of Myoglobin

2008
Protein 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
openaire   +3 more sources

Myoglobin

Acta Medica Scandinavica, 1979
B, Scherstén, D, Ursing, G, Jonsson
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Myoglobin

2018
Alfred H. Free, Helen M. Free
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Plasmonic DNA hotspots made from tungsten disulfide nanosheets and gold nanoparticles for ultrasensitive aptamer-based SERS detection of myoglobin

Microchimica Acta, 2018
Munish Shorie   +5 more
semanticscholar   +1 more source

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