Results 211 to 220 of about 18,427 (259)
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The effect of acidification on myofibrillar proteins

Meat Science, 1994
Isolated myofibrillar proteins of mutton, beef and chicken were treated with an acidulent to give various pH values and stored at 5°C for 20 h before analysing the proteins using sodium dodecylsulphate polyacrylamide gel electrophoresis. It was found that protein degradation occurred below pH 4·5, with a decrease in band intensity of all major ...
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The solubilization of myofibrillar proteins by calcium ions

Meat Science, 1991
The effect of elevated levels (30 mm) of Ca(2+) and other divalent metals ions on rabbit psoas myofibrils was studied to determine whether these caused solubilization of structural proteins and if so whether the effect was due to salting-in or to proteolytic fragmentation resulting from activation of calpains.
M A, Taylor, D J, Etherington
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Heterogeneous Turnover of Myofibrillar Protein

Nature New Biology, 1972
TO investigate the heterogeneity of turnover of proteins of the myofibril, we developed “a continuous double isotope method” which is a modification of the continuous isotope administration method. The assumptions involved in the use of the double isotope method, proposed by Schmike1, are not applicable in the case of proteins of the myofibril because ...
RYUHEI FUNABIKI, R. G. CASSENS
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Myofibrillar protein pattern in experimental myotonia in rats

Journal of the Neurological Sciences, 1976
Experimental myotonia was induced in rats by long-term administration of 20,25-diazacholesterol. Electrophysiological, morphological and biochemical investigations were carried out on m. soleus, m. extensor digitorum longus and m. gastrocnemius. The effect of 20,25-diazacholesterol administration on myofibrillar proteins was studied and a significant ...
I, Niebrój-Dobosz   +2 more
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Dephosphorylation enhances postmortem degradation of myofibrillar proteins

Food Chemistry, 2018
Protein degradation is primarily responsible for postmortem meat tenderization, which might be affected by phosphorylation. The objective of this study was to investigate the effect of phosphorylation on myofibrillar proteins degradation in muscle during postmortem. Here we modulated the phosphorylation status of protein by protein kinase inhibitor and
Zheng Li   +4 more
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Myofibrillar protein synthesis in young and old men

American Journal of Physiology-Endocrinology and Metabolism, 1993
We tested the hypothesis that healthy older men (> 60 yr old) have a slower rate of myofibrillar protein synthesis than young men (< 35 yr old). Myofibrillar protein synthesis was determined by the in vivo incorporation of L-[1-13C]leucine into myofibrillar proteins obtained by muscle biopsy. Subjects were eight young (21-31 yr) and eight older (
S, Welle   +3 more
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In vitro non-enzymatic glycosylation of myofibrillar proteins

International Journal of Biochemistry, 1993
1. 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, 1985
Lysosomes 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

1994
Very 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, 1989
Myocardial 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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