The pH optimum was the same in canine tissue for cardiac and skeletal muscle myosin; when myosin was activated by monovalent cations, the pH optimum was 7.5 while activation of myosin by divalent cations gave a pH optimum of 5.5. Protons were needed for divalent cation activation of myosin. With changes in pH there were concomitant changes in the apparent affinity of enzyme for substrate (S 0.5), such that with a decrease in pH there was an elevation in K+- or NH4+ -activated myosin's apparent affinity for adenosine triphosphate (ATP), and at the same time a decrease in Vmax values of myosin. The converse was true with the divalent cations, Ca++ and Mn++; here with a decrease in pH there was a concomitant decrease in apparent affinity of myosin for ATP, and at the same time an increase in the enzymatic Vmax values. It appeared that hydrogen ions affected the apparent affinity of myosin for substrate and this in turn affected the rate-limiting step in ATPase reaction. Addition of monovalent cations to the divalent cation activating system lowered the activity of myosin, and the converse was true: divalent cations lowered the activity of myosin when activated by monovalent ones in a monovalent cation activating system.
|Original language||English (US)|
|Number of pages||11|
|Journal||Recent advances in studies on cardiac structure and metabolism|
|State||Published - Dec 1 1975|
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