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Muscle proteins

2004
Proteins within the muscle matrix play an essential role in the quality attributes of cooked meat, such as tenderness, juiciness, and mouthfeel. In processed meats, salt- and phosphate-extracted myofibrillar proteins, which are superior gelling, fat-emulsifying, and water-binding agents, are largely responsible for the product textural properties.
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The action of a muscle proteinase on the myofibrillar proteins of bovine muscle

Journal of the Science of Food and Agriculture, 1974
AbstractMyofibrillar proteins from bovine muscle have been treated with a Ca2+ activated muscle proteinase and the consequent changes in these proteins have been examined by various techniques. Tropomyosin, α‐actinin and troponin were substrates for the enzyme, the last losing its property of inhibiting actomyosin ATPase in the absence of Ca2+ ions ...
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Fixation of muscle proteins with antibodies

Biochimica et Biophysica Acta, 1960
Abstract Treatment of myofibrils with antibodies, prepared against purified muscle proteins, increases the phase density of well-defined parts of the sarcomere. These parts become insoluble and resist extraction by strong salt solutions. The resulting patterns are different with various antibodies and characteristic to the specific antibody used ...
Howard Holtzer   +3 more
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Insulin and protein synthesis in muscle

Archives of Biochemistry and Biophysics, 1970
Abstract Insulin stimulates in vitro the incorporation of labeled amino acid into muscle protein. A study of this phenomenon has been carried out in which various incubation conditions have been varied. The insulin stimulatory effect is lost when sodium ion is removed from the medium, when the amino acid concentration of the medium is increased to ...
Samuel Goldstein, William J. Reddy
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Protein Assemblies in Muscle

1972
The myofibril, the contractile unit of muscle, may be thought of as a highly concentrated suspension of proteins (~20%) enveloped by a membranous sac. Some of these proteins are globular in conformation, such as actin or troponin; some are highly α-helical, such as tropomyosin; while the most abundant protein, myosin, combines both globular and fibrous
S. Lowey, S. Lowey
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Muscle proteins and muscular dystrophy

Current Opinion in Cell Biology, 1989
In recent years, muscle biology has been transformed by the use of recombinant DNA technology. A result of this approach of great practical importance is the localization on the human X-chromosome of the site of mutation(s) causing Duchenne muscular dystrophy (DMD). DMD is a devastating disease causing degeneration of skeletal muscle fibres and leading
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Testosterone and Muscle Protein Metabolism

Mayo Clinic Proceedings, 2000
This presentation discusses recent investigations into testosterone's effects on muscle protein metabolism. Protein synthesis is the principal end point, but protein breakdown and the availability of an amino acid pool are important to the process of net muscle protein synthesis.
Arny A. Ferrando   +3 more
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In vitro Methylation of Muscle Proteins

Nature, 1969
3-METHYL HISTIDINE is a normal amino-acid component of myosin from adult muscle1 and of actin1,2. But whereas 3-methyl histidine occurs in actin isolated from adult and foetal muscle it is absent from myosin isolated from skeletal muscle of the foetal rabbit.
S. V. Perry, Madeleine F. Hardy
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Interactions of muscle proteins

2015
This thesis commences with two contributions to the development of methodology for the study of macromolecular interactions. Firstly, a procedure is described whereby results obtained by gel chromatography for the binding of charged ligands to macroions are corrected automatically for the Donnan redistribution of small ions between the mobile and ...
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Myofibrillar Proteins of Skeletal Muscle

1971
Publisher Summary Muscle is a highly integrated chemical machine. One of the most impressive aspects of this integration is the ability to increase the rate of energy utilization by approximately 2500-fold within milliseconds. This efficient transduction of chemical into mechanical energy occurs through the subtleties of the interactions of myosin ...
T. Fukazawa, E. J. Briskey
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