Results 341 to 350 of about 7,838,731 (404)
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The action of a muscle proteinase on the myofibrillar proteins of bovine muscle
Journal of the Science of Food and Agriculture, 1974AbstractMyofibrillar proteins from bovine muscle have been treated with a Ca2+ activated muscle proteinase and the consequent changes in these proteins have been examined by various techniques. Tropomyosin, α‐actinin and troponin were substrates for the enzyme, the last losing its property of inhibiting actomyosin ATPase in the absence of Ca2+ ions ...
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Heat Coagulation of Muscle Proteins
Nature, 1945A CHANGE in pH when proteins are denatured has been reported by other workers1,2. When making observations of the change in pH of meat resulting from heat coagulation, we were struck both by the magnitude and by the variability of the change. Muscle is a highly buffered system3, and a change such as that observed, for example, from 5·6 to 5·9 ...
E. C. Bate-Smith, J. R. Bendall
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Functionality of muscle proteins in gelation mechanisms of structured meat products.
Critical reviews in food science and nutrition, 1990Recent advances in muscle biology concerning the discoveries of a large variety of proteins have been described in this review. The existence of polymorphism in several muscle proteins is now well established.
Ali Asghar +3 more
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Creatine as an indicator of net muscle proteins
, 1981Creatine and creatinine levels in different cuts of pork, beef, veal and lamb have been estimated and expressed in relation to the content of total proteins (N × 6.25) and net muscle proteins (N × 6.25 minus hydroxyproline × 8).
Z. Dvořák
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Fixation of muscle proteins with antibodies
Biochimica et Biophysica Acta, 1960Abstract Treatment of myofibrils with antibodies, prepared against purified muscle proteins, increases the phase density of well-defined parts of the sarcomere. These parts become insoluble and resist extraction by strong salt solutions. The resulting patterns are different with various antibodies and characteristic to the specific antibody used ...
Howard Holtzer +3 more
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1972
The myofibril, the contractile unit of muscle, may be thought of as a highly concentrated suspension of proteins (~20%) enveloped by a membranous sac. Some of these proteins are globular in conformation, such as actin or troponin; some are highly α-helical, such as tropomyosin; while the most abundant protein, myosin, combines both globular and fibrous
S. Lowey, S. Lowey
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The myofibril, the contractile unit of muscle, may be thought of as a highly concentrated suspension of proteins (~20%) enveloped by a membranous sac. Some of these proteins are globular in conformation, such as actin or troponin; some are highly α-helical, such as tropomyosin; while the most abundant protein, myosin, combines both globular and fibrous
S. Lowey, S. Lowey
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Insulin and protein synthesis in muscle
Archives of Biochemistry and Biophysics, 1970Abstract Insulin stimulates in vitro the incorporation of labeled amino acid into muscle protein. A study of this phenomenon has been carried out in which various incubation conditions have been varied. The insulin stimulatory effect is lost when sodium ion is removed from the medium, when the amino acid concentration of the medium is increased to ...
Samuel Goldstein, William J. Reddy
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Functional properties of muscle proteins in processed poultry products
, 2001Introduction Muscle proteins Myofibrillar proteins Sarcoplasmic and stroma proteins Role of proteins in comminuted products Role of proteins in formed products Protein-water interactions Effect of salt and pH on protein-water interactions Processing ...
Denise M Smith
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Reduced synthesis of muscle proteins in chronic renal failure.
American Journal of Physiology. Endocrinology and Metabolism, 2000Muscle wasting and weakness occur frequently in patients with chronic renal failure. The mechanism(s) by which these abnormalities occur is unclear. We hypothesized that such findings were due to defective muscle protein synthesis.
Deborah Adey +3 more
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Relationship between thermal denaturation of porcine muscle proteins and water-holding capacity
, 2002: Differential scanning calorimetry was used to investigate denaturation characteristics of pork muscle proteins from carriers and noncarriers of the RN-gene.
Y. Deng +6 more
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