Enzymatic properties of myosin ATPase from abalone Haliotis discus smooth muscle.

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  • アワビミオシンＡＴＰａｓｅの酵素的性質
  • アワビミオシシ ATPase ノ コウソテキ セイシツ

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Abstract

Abalone myosin was prepared by a more speedy method. The properties of this myosin were studied under various conditions with regard to their Mg-, Ca-, EDTA-ATPase and actin-activated ATPase activities.<br> The properties of abalone myosin ATPase were almost similar to those of scallop myosin, though the following differences were observed.<br> 1. Ca-sensitivity of abalone myosin was higher than that of scallop myosin.<br> 2. At neutral pH and 25°C, enzymatic activities were lower than those of scallop myosin, except in EDTA-ATPase activity.<br> 3. PH activity curve of Mg-ATPase activity at low ionic condition was an U-shaped curve in contrast to the biphasic curve in scallop myosin. PH activity curves of EDTA-ATPase activity were bell-shaped curves with a peak at pH around 8.0, which was higher than that of scallop my-osin.<br> 4. Arrhenius plots of abalone myosin ATPase activities showed no bending between 5-30°C which was different from that of scallop myosin.<br> The spccific cystein residue, so-called SHI was not dotected by the treatment of abalone myosin with NEM or PCMB.

Journal

  • NIPPON SUISAN GAKKAISHI

    NIPPON SUISAN GAKKAISHI 53 (7), 1243-1249, 1987

    The Japanese Society of Fisheries Science

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