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International Journal of Biochemistry, 1992
1. The mode of degradation of myofibrillar proteins and the structural changes in myofibrils due to the action of cathepsin B highly purified from rabbit skeletal muscle were studied. 2. Cathepsin B degraded myosin heavy chain, actin and troponin T, but not alpha-actinin, tropomyosin, troponin I or troponin C among myofibrillar proteins. 3. Cathepsin B
M, Matsuishi +3 more
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1. The mode of degradation of myofibrillar proteins and the structural changes in myofibrils due to the action of cathepsin B highly purified from rabbit skeletal muscle were studied. 2. Cathepsin B degraded myosin heavy chain, actin and troponin T, but not alpha-actinin, tropomyosin, troponin I or troponin C among myofibrillar proteins. 3. Cathepsin B
M, Matsuishi +3 more
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Phosphorylation of cardiac myofibrillar proteins.
Recent advances in studies on cardiac structure and metabolism, 1978The P light chain of cardiac myosin is phosphorylated and dephosphorylated by highly specific enzymes. These reactions take place in the beating rabbit heart and there is evidence that dephosphorylation of the light chain occurs during the inotropic response produced by adrenaline.
H A, Cole +4 more
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Lobster Muscle Proteasome and the Degradation of Myofibrillar Proteins
Enzyme and Protein, 2017The lobster proteasome is primarily a cytosolic enzyme in crustacean striated muscles, although a small amount (<1 % of total) occurs in aggregates associated with invaginations of the cell membrane. The complex exists in vitro in three distinct catalytic states (basal, SDS-activated, and heat-activated forms) which have identical subunit ...
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Metabolism of myofibrillar proteins in the normal and hypertrophic heart
Basic Research in Cardiology, 1977The pathways of myofibrillar assembly and degradation were studied in normal heart and during developing hypertrophy by two independent methods: amino acid incorporation kinetics and the double isotope technique. The validity and sensitivity of both methods were evaluated by computer analysis of data for which leucyl-tRNA was used as a protein ...
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International Journal of Biological Macromolecules
The pH buffering capacity is an important functionality of muscle proteins, and muscle foods are susceptible to being oxidized during storage and processing. In order to study the effect of oxidation on the pH buffering capacity of myofibrillar proteins, myofibrils extracted from snakehead fish (Channa argus) were oxidized with H2O2.
Qingqing, Yu +5 more
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The pH buffering capacity is an important functionality of muscle proteins, and muscle foods are susceptible to being oxidized during storage and processing. In order to study the effect of oxidation on the pH buffering capacity of myofibrillar proteins, myofibrils extracted from snakehead fish (Channa argus) were oxidized with H2O2.
Qingqing, Yu +5 more
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Insight into the oil polarity impact on interfacial properties of myofibrillar protein
Food Hydrocolloids, 2022Xue Zhao, Guanghong Zhou
exaly
Myofibrillar Proteins in the Developing Hearta
Annals of the New York Academy of Sciences, 1990R, Zak +5 more
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Effects of ultrasound emulsification on the properties of pork myofibrillar protein-fat mixed gel
Food Chemistry, 2021Lei Zhou +2 more
exaly
A Study of γ Component, a Myofibrillar Protein
The Journal of Biochemistry, 1977G, Ashiba, S, Watanabe
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