Results 231 to 240 of about 4,202 (274)
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Cardiac myosin Phylogenic and pathological changes

1977
Several proteins of the sarcomere differ from one muscle to the other, but it is also becoming evident that cardiac myosin, tropomyosin and troponin are species specific. Moreover, several properties of cardiac myosin could be modified under the influence of thyroxine, exercise, or overloading.
B, Swynghedauw, K, Schwartz, J J, Léger
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Studies on cardiac myosin light chains: Comparison of the sequences of cardiac and skeletal myosin LC-2

Biochemical and Biophysical Research Communications, 1977
Abstract Partial sequence analysis of bovine cardiac myosin LC-2 indicates that it is closely related to LC-2, the “DTNB light chain” of skeletal muscle myosin. The results suggest that myosins from a variety of sources have related light chains of two distinct types, although the sizes and properties of the light chains can vary substantially.
J J, Léger, M, Elzinga
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The Calmodulin-Dependent Phosphorylation of Cardiac Myosin

1985
Cardiac myosin light chains are phosphorylated in vivo and in vitro. The enzyme myosin light-chain kinase, has been purified and found to be very specific for cardiac myosin light chains. Experiments with skinned cardiac fibers suggest that phosphorylation of myosin light chain-2-decreases ATP consumption, presumably by lowering the cross-bridge cycle.
F, Hofmann, M, Zimmer
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Methylation of canine cardiac myosin in culture

Experientia, 1980
N epsilon, N epsilon, N epsilon, trimethyllysine and an unidentified methylated amino acid which co-electrophoresed and co-chromatographed with the hydrolysis product of S-adenosyl-L-methionine, occur in fetal canine cardiac myosin and are isotopically labeled in vitro with S-adenosyl-L-(methyl 3H) methionine between the 10th and 12th day of culture.
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Ca-independent regulation of cardiac myosin

1987
Calcium-independent regulation of the contractile proteins of cardiac muscle has been studied using hyperpermeable cells from rat ventricles and sections of quickly frozen rat hearts. These preparations have been used to study maximum Ca-activated force, myosin ATPase activity and the maximum velocity of unloaded shortening.
S, Winegrad   +5 more
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Cardiac and skeletal muscle myosin polymorphism

Medicine & Science in Sports & Exercise, 1986
Skeletal muscles, unlike cardiac tissue, express several myosin isozymes during development which differ in primary structure from adult myosin. Monoclonal antibodies have shown the presence of at least two embryonic myosins, followed by a post-hatch myosin that persists until the appearance of adult myosin in chicken pectoralis muscle.
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Cardiac Myosin Light Chains

Laboratory Medicine, 1992
The detection of circulating levels of cardiac myosin light chains (MLCs) recently has been proposed as a new biochemical marker of myocardial damage. In patients with unstable angina and acute myocardial infarction, measurement of MLCs seems to provide diagnostic information that differs from that obtained by determination of traditional cardiac ...
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Cardiac Myosin in Heart Overloading

1981
The heart, like most types of tissues, can adapt to envirommental factors and, more specifically, to its load. Overloading a heart as well as changing its initial length may increase work by means of two successive adaptational processes: (1) immediately by bringing the muscle’s own mechanical properties into play and (2) at a later stage by changing ...
B. Swynghedauw   +5 more
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Cardiac myosin and autoimmune myocarditis.

Ciba Foundation symposium, 1988
Infection with type 3 of the group B Coxsackieviruses (CB3) sometimes leads to the development of myocarditis in humans. Circumstantial evidence in the form of heart-reactive antibodies in these cases of human myocarditis suggests that the later phases of the disease may be due to autoimmunization. Since human myocarditis is a relatively rare sequel to
N R, Rose   +7 more
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Hormonal influences on cardiac myosin ATPase activity and myosin isoenzyme distribution

Molecular and Cellular Endocrinology, 1984
It has been recognized for a long time that changes in hormone secretion can influence cardiac function; however, the biochemical basis for these changes has only recently been clarified. In this review the influences of hormonal status on the contractile protein myosin is discussed. Myosin has a rod-like portion and a globular head and consists of two
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