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Myoglobin Analysis

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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ChemInform Abstract: Nitric Oxide and Myoglobins

ChemInform, 2002
AbstractChemInform 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, 1948
ALTHOUGH 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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Myoglobin in Myocardial Infarction

Annals of Internal Medicine, 1978
Excerpt To the editor: With regard to the article by Dr. Roberts in the December issue (Ann Intern Med 87:788-789, 1977) on the comparative values of MB-creatine kinase and myoglobin in patients wi...
L J, Kagen, S, Scheidt, R, Roberts
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The crystal structure of myoglobin. VI. Seal myoglobin

Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences, 1960
Myoglobin from the common seal ( Phoca vitulina ) when crystallized from ammonium sulphate forms monoclinic crystals with space group the unit cell, a = 57·9Å, b = 29·6Å, c = 106·4Å, β = 102°15', contains four molecules ...
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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].
Zhen Yan   +3 more
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Structural dynamics of myoglobin

Biophysical Chemistry, 2000
Conformational fluctuations have been invoked to explain the observation that the diffusion of small ligands through a protein is a global phenomenon, as suggested (for example) by the oxygen induced fluorescence quenching of buried tryptophans. In enzymes processing large substrates, a channel to the catalytic site is often seen in the crystal ...
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Myoglobin

Acta Medica Scandinavica, 1979
B, Scherstén, D, Ursing, G, Jonsson
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In Vitro Responses of Myoglobin-Primed Lymph Node Cells to Myoglobin and Myoglobin Synthetic Antigenic Peptides

1978
The ultimate objective of the newer immunology is to understand various immune responses and reactions in cellular and molecular terms. The relevant molecules include various antigenic determinants, receptors and antigen-binding molecules on lymphocytic surfaces, molecules produced and secreted by lymphocytes, and lymphocytic surface molecules that ...
R. P. Pelley   +6 more
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Haemoglobins and Myoglobins

1975
The solubility of O2 in aqueous media is relatively low; one litre of pure water in equilibrium with air at 20°C and atmospheric pressure dissolves 6.59 cm3 of O293, which corresponds to a 3 × 10−4M solution. This limits the rate of diffusion of O2 from the surface of an organism and also the rate at which O2 can be delivered by a circulatory system ...
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