Cardiac myosin adenosinetriphosphatase activity. Modifying factors and comparison with skeletal muscle myosin adenosinetriphosphatase activity.

Abstract

Cardiac myosin prepared by any one of a number of modifications of the basic Szent-Gyorgyi method and cardiac myosin prepared by the lithium chloride-ammonium sulfate technique differ in two important respects: 1) Szent-Gyorgyi-prepared myosin solutions are inhomogeneous by both chemical and immunologic criteria; 2) the ATPase activity of Szent-Gyorgyi-prepared myosin is low in comparison to lithium chloride-ammonium sulfate prepared cardiac myosin. Evidence is presented in this paper showing that the reduced ATPase activity of Szent-Gyorgyi-prepared cardiac myosin is the result of inhibition of the enzyme, possibly by a nucleotide contaminant, and a "diluting" effect of other nitrogen-containing contaminants of low specific activity. Many earlier studies indicate that cardiac and skeletal muscle myosin prepared by the Szent-Gyorgyi method differed strikingly in their ATPase activities. Comparison of lithium chloride-ammonium sulfate prepared cardiac and skeletal muscle myosin shows that skeletal muscle myosin has a slightly but significantly higher ATPase activity than canine cardiac myosin. A methodologic error was not excluded as the cause of this discrepancy. In a number of other characteristics, canine cardiac and skeletal muscle myosin ATPase activity was virtually identical.