Effect of Ultrasonics on the Adenosine Triphosphatase Activity and Actin-binding Ability of L-Myosin and Heavy Meromyosin

Abstract

ASAKURA¹ recently discovered that F-actin retains its native properties under ultrasonic vibration. In a more recent investigation Ohnishi and Ohnishi² reported that the ATPase activity of glycerinated muscle fibres increases under the same conditions. It would appear, therefore, that both structural muscle proteins are resistant to ultrasonic treatment. Physicochemical studies on the effect of ultrasonics on L-myosin and the meromyosins have shown in this laboratory that L-myosin and heavy meromyosin were readily fragmented, whereas light meromyosin was relatively resistant to vibration³. The effect of ultrasonics on the biochemical properties of L-myosin and heavy meromyosin will be described in this paper.