According to the method adopted for striated adductor muscles of scallop, purified actins were successfully prepared from the smooth adductor muscles of surf-clam,
Spisula sachalinensis, and scallop,
Patinopecten yessoensis.
1) Crude G-actins, extracted by the method of STRAUB, were found to be contaminated with a small amount of tropomyosin and paramyosin. These crude actins were highly purified by the method of SPUDICH
et al. The yields of pure G-actins were 400mg and 150mg from 100g of smooth adductor muscles of surf-clam and scallop, respectively.
2) G-actin preparations were polymerized by the addition of 0.1M KCl; they had a viscosity similar to that of rabbit skeletal F-actin.
3) Reconstituted actomyosins from smooth adductor F-actin and rabbit skeletal myosin showed the characteristic properties of actomyosin, i.e. superprecipitation, high ATP-sensitivities, elevation of Mg
2+-ATPase activity, and stabilization of Ca
2+-ATPase activity.
4) From these results, it is concluded that the biological activities of actins from the smooth adductor muscles of surf-clam and scallop are essentially the same as those of actins from the striated adductor muscles of scallop and the skeletal muscles of rabbit.
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