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Correction to 'A single bout of prior resistance exercise attenuates muscle atrophy and declines in myofibrillar protein synthesis during bed-rest in older men'. [PDF]
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Phosphorylation of the Myofibrillar Proteins
Annual Review of Physiology, 1980In muscle, protein phosphorylation takes place in both the sarcoplasm and the myofibrils. This review deals only with those myofibrillar proteins that can be phosphorylated-i.e. myosin light chain and in a few cases the heavy chain, the inhibitory and tropomyosin-binding subunits of troponin, and tropomyosin.
M, Bárány, K, Bárány
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Note on differentiation of myofibrillar proteins
Journal of the Science of Food and Agriculture, 1970AbstractThe detection of qualitative differences between the myofibrillar proteins of muscles, which superficial examination would classify as similar on the basis of their ‘redness’ or ‘whiteness’, emphasises the need for more subtle criteria for understanding meat quality.
A, Champion, A L, Parsons, R A, Lawrie
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On cryodenaturation of chicken myofibrillar proteins
Cryobiology, 1968Summary Myofibrillar protein preparations isolated from chicken pectoralis major containing 81 to 95% protein and 3 to 4% lipids, on dry weight basis, were used as a model system to study the nature of protein and lipid changes occurring as a result of frozen storage.
A W, Khan, E, Davidkova, L, Van den Berg
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Ionic Strength and Myofibrillar Protein Solubilization
Journal of Animal Science, 1987Myofibrils from bovine longissimus muscle were obtained at 2 h postmortem and incubated in .10 to .35 M ionic strength buffers under various conditions in vitro. Increasing ionic strength or increasing the incubation time from 1 to 72 h decreased the turbidity of suspensions of myofibrils and increased myofibrillar solubilization (P less than .01 for ...
F Y, Wu, S B, Smith
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Interaction of Fish Myoglobin and Myofibrillar Proteins
Journal of Food Science, 2008ABSTRACT: Interactions between fish myoglobin (Mb) and myofibrillar proteins were investigated in a Mb‐natural actomyosin (NAM) model at 4 °C. Increases in metmyoglobin (MetMb) formation and the relative content of bound Mb were observed, as were decreases in whiteness and Ca 2+
M, Chaijan +4 more
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Myofibrillar Proteins of Skeletal Muscle
1971Publisher 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 ...
E J, Briskey, T, Fukazawa
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The solubilization of myofibrillar proteins by calcium ions
Meat Science, 1991The 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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The effect of acidification on myofibrillar proteins
Meat Science, 1994Isolated 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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