Results 231 to 240 of about 21,460 (265)
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In vitro non-enzymatic glycosylation of myofibrillar proteins
International Journal of Biochemistry, 19931. Glycation is non-enzymatic modification of proteins by sugars in which not only structural but also biological properties of proteins are altered. 2. Our in vitro experiments show that incubation of myofibrillar proteins with ribose results in sugar attachment to proteins and at the same time myofibrillar ATPase activity is lowered. 3.
I, Syrovy, Z, Hodny
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The role of lysosomes in the degradation of myofibrillar and non-myofibrillar proteins in heart.
Progress in clinical and biological research, 1985Lysosomes are presumed to be involved in protein degradation in heart, but their exact role is poorly understood. Several interventions that are known to alter cardiac proteolysis (e.g., insulin) also produce lysosomal changes that might account for the observed changes in protein degradation; but many other interventions appear not to do so.
K, Wildenthal, J R, Wakeland
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The Myofibrillar Proteins in Seafoods
1994Very concise and informative reviews on the myofibrillar proteins have been published by Maruyama (1985), Squire and Vibert (1987), Nakai and Li-Chan (1988), and Morrissey, Mulvihill, and O’Neill (1987). They describe not only the chemical structure, properties, and location of myosin and actin, of the regulatory proteins, and of the scaffold proteins ...
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Calcium-Sensitivity Modulation of Cardiac Myofibrillar Proteins
Journal of Cardiovascular Pharmacology, 1989Myocardial contractile force may be altered not only by changing intracellular free Ca2+ but also by increasing or decreasing the calcium responsiveness of the myofilaments. The latter effect may be due to interventions that decrease the calcium affinity of troponin C, such as intracellular acidosis or factors that act "downstream" of the calcium ...
J C, Rüegg, I, Morano
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Food Chemistry
The effect of magnetic field on the properties of emulsified gels containing myofibrillar protein (MP-emulsified gels) with different salt concentration (0, 0.2, 0.4, 0.6 mol/L) were investigated. The results demonstrated that the magnetic field treatment (4 °C, 3.8 mT, 3 h) made the emulsion droplets smaller and more uniform.
Qianwen, Jiang +7 more
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The effect of magnetic field on the properties of emulsified gels containing myofibrillar protein (MP-emulsified gels) with different salt concentration (0, 0.2, 0.4, 0.6 mol/L) were investigated. The results demonstrated that the magnetic field treatment (4 °C, 3.8 mT, 3 h) made the emulsion droplets smaller and more uniform.
Qianwen, Jiang +7 more
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Mechanisms of Degradation of Myofibrillar and Nonmyofibrillar Protein in Heart
1983The degradation of cardiac proteins is known to be altered by many physiological and pathological interventions, but the precise intracellular processes that regulate proteolysis and the relative roles of different proteolytic pathways in degrading different classes of protein remain poorly understood.
J M, Ord +3 more
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Myofibrillar protein degradation after eccentric exercise
Experientia, 1984Male rats were run downhill for 90 minutes (nonexhaustive). Following the exercise, muscle protein degradation was increased, as determined by urinary 3-methylhistidine. However, minimal changes were observed in the relative percentage of the minor myofibrillar proteins and in the protease calcium activated factor in the long head of the triceps ...
A C, Snyder +5 more
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Quantification of beef myofibrillar proteins by SDS-PAGE
Meat Science, 1995A semi-quantitative determination of beef myofibrillar proteins using sodium, dodecyl sulphate polyacrylamide gel electrophoresis is described. Bovine serum albumin was used as internal standard. Results indicate a linear relationship between densitometric readings after staining with Coomassie brilliant blue R(250) and protein content.
E, Claeys +3 more
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F-Protein, a myofibrillar protein interacting with myosin.
Journal of biochemistry, 1980F-Protein has an amino acid composition distinctively different from those of myofibriller proteins so far reported to be of similar chain weight: M-protein component II, alpha-actinin, and AMP deaminase. Its molecular weight was estimated to be 121,000 by sedimentation equilibrium in 0.3 M KCl, 10 mM potassium phosphate, pH 6.5.
M, Miyahara, K, Kishi, H, Noda
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