Myosin and cardiac hypertrophy
Lêger, J.J.; Schwartz, K.; Swynghedauw, B.
Pathologie-Biologie 25(2): 75-80
1977
ISSN/ISBN: 0369-8114 PMID: 139588 Document Number: 111435
Myosin, which represents 1/4 of the weight of cardiac proteins, comprises virtually the entire composition of the dense filament of myofibrils. Its enzyme activity expresses the liberty necessary for contraction. The amino acid composition and sequence of cardiac myosin differs from that of skeletal muscle myosin, and differs from animal to animal. The sequence of a single peptide isolated from the heavy myosin chains is characteristic for each animal species. Incubation of rabbit and dog myosin at an alkaline pH for 10 min causes a large decrease in enzyme activity, but rat cardiac myosin is unaffected by this treatment. There is a similar difference between these animal species in response to N-ethylmaleimide, which reacts with sulfur linkages. K-dependent cardiac myosin activity is the same for different animals, but values differ for Ca-dependent activity in man, dog, guinea pig, rat and mouse.