Results 161 to 170 of about 17,601 (220)
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Phosphorylation of the Myofibrillar Proteins

Annual Review of Physiology, 1980
In 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
openaire   +2 more sources

Myofibrillar protein degradation after eccentric exercise

Experientia, 1984
Male 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
openaire   +2 more sources

Note on differentiation of myofibrillar proteins

Journal of the Science of Food and Agriculture, 1970
AbstractThe 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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Ionic Strength and Myofibrillar Protein Solubilization

Journal of Animal Science, 1987
Myofibrils 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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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 ...
E J, Briskey, T, Fukazawa
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On cryodenaturation of chicken myofibrillar proteins

Cryobiology, 1968
Summary 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
openaire   +2 more sources

Contribution of Sarcoplasmic Proteins to Myofibrillar Proteins Gelation

Journal of Food Science, 2012
Abstract:  Surimi, a refined protein extract, is produced by solubilizing myofibrillar proteins during the comminuting and salting stages of manufacturing. The resulting paste gels on heating to produce kamaboko or a range of analog shellfish such as crab claw, filament sticks, fish mushroom, and so on.
Ali, Jafarpour, Elisabeth M, Gorczyca
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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
openaire   +1 more source

Interaction of Fish Myoglobin and Myofibrillar Proteins

Journal of Food Science, 2008
ABSTRACT:  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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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
openaire   +2 more sources

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