ホタテガイ閉殻筋横紋部ミオシンのイオン交換クロマトグラフィーによる精製

抄録

Myosin was prepared form the striated adductor muscle of the giant ezo scallop, Patinopecten yessoensis, by the original method of BÁRÁNY et al.
It was found that the present myosin preparation was effectively solubilized in a 0.06M Na-pyrophosphate solution (pH 7.5) but incompletely in a 0.04M solution (pH 7.5).
Scallop myosin was, therefore, applied on DEAE-sephadex A-50 column chromatography introducing the 0.06M Na-pyrophoshate solution (pH 7.5) as solvent. The elution profiles of the scallop myosin were very similar to those of the rabbit and fish myosin monomer. The Ca²⁺-ATPase activity of the eluted myosin was not improved by the ion-exchange chromatography, although the contaminants such as paramyosin and actin were effectively eliminated form this preparation.
To avoid the denaturation of myosin during the time-consuming column chromatography, the batchwise ion-exchange method was successfully adopted to purify the scallop myosin. The purified myosin, thus obtained, showed a Ca²⁺-ATPase activity (1.13-1.15 μmoles Pi iberation/min•mg of protein) approximately 1.5 fold higher compared to that of the original myosin.