Results 161 to 170 of about 1,546,271 (206)
Some of the next articles are maybe not open access.
Heterogeneous Turnover of Myofibrillar Protein
Nature New Biology, 1972TO 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
Dephosphorylation enhances postmortem degradation of myofibrillar proteins
Food Chemistry, 2018Protein 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
Myofibrillar protein pattern in experimental myotonia in rats
Journal of the Neurological Sciences, 1976Experimental 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
openaire +2 more sources
Myofibrillar protein synthesis in young and old men
American Journal of Physiology-Endocrinology and Metabolism, 1993We 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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +1 more source
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
openaire +2 more sources
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 ...
openaire +1 more source
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
openaire +2 more sources
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
openaire +2 more sources