Letter | Published:

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

Naturevolume 199pages694695 (1963) | Download Citation



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.

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  1. Institute for Muscle Disease, Inc., New York, 21

    • M. BÁRÁNY
    • , K. BÁRÁNY


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