Results 211 to 220 of about 6,676 (255)

Myosin from cardiac muscle

Biochimica et Biophysica Acta, 1951
Abstract Myosin from cardiac muscle was prepared which seems to be free from contamination by F-actin. The electrophoretic mobility and sedimentation constant are the same as for crystallized myosin from skeletal muscle, but the sedimentation constant has another concentration dependence.
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Biochemical characteristics of human cardiac myosin

Journal of Molecular and Cellular Cardiology, 1977
Abstract Myosin was purified from the left ventricles of eight patients. Samples of the ventricle were obtained immediately after the death of three patients whereas the rest were obtained from 2 1 2 to 20 h after the death. Human cardiac myosin, like the cardiac myosin from other mammalian species has only two light chains. The corresponding
A, Malhotra, A, Bhan, J, Scheuer
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β-Adrenergic regulation of cardiac myosin

Canadian Journal of Physiology and Pharmacology, 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 calcium-activated force, myosin ATPase activity, and the maximum velocity of unloaded shortening.
S, Winegrad, G, McClellan, A, Weisberg, L E, Lin, S, Weindling, R, Horowits   +5 more
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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 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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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, G, McClellan, A, Weisberg, L E, Lin, S, Weindling, R, Horowits   +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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Internal flexibility of cardiac myosins

Journal of Thermal Analysis, 1996
Conventional and saturation transfer electron paramagnetic resonance spectroscopy (EPR and ST EPR) and differential scanning calorimetry (DSC) were used to study the motional dynamics and segmental flexibility of cardiac myosins. Cardiac myosins isolated from bovine and human heart muscle were spin-labelled with isothiocyanate- or maleimide-based probe
D. LŐrinczy, J. Belágyi
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T Cells in Cardiac Myosin-Induced Myocarditis

Clinical Immunology and Immunopathology, 1993
Autoimmune myocarditis induced by immunization with cardiac myosin can be seen as a virus-free system to analyze the immunopathological mechanisms of certain forms of postinfectious heart disease. Immunodepletion studies have shown that in A.SW mice myosin-induced myocarditis is mediated by both CD4+ and CD8+ cells. The CD4+ subset is at least required
N, Neu, C, Pummerer, T, Rieker, P, Berger   +3 more
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Monoclonal Antibodies Against Cardiac Myosin Heavy Chain

Hybridoma, 1990
Three mouse IgG1 monoclonal antibodies (MAbs), named FA1, FA2, and FA3, against cardiac myosin heavy chain (MHC) with high specificity have been obtained. The immunogen used to generate these MAbs was the high-salt- and detergent-insoluble fraction of adult rat myocardial tissue.
J P, Jin, M L, Malik, J J, Lin
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