Abstract
The smooth adductor myosin of the scallop Patinopecten yessoensis was examined on its physico-chemical and enzymatic properties. It was found to have a sedimentation constant (S020, W) of 6.65 S, a molecular weight of about 450, 000, and an intrinsic viscosity of 1.76 dl/g. It is completely soluble in 0.25M KCl and salts out with ammonium sulfate between 34-40% saturation. It exhibits an absorption maximum at 277 nm with E1%1cm 5.2. In amino acid composition, it is rich in Glu and Asp and poor in several amino acids such as His and Trp. In the presence of 0.5M KCI, it exhibits two pH optima at around 7 and 9 for Ca2+- ATPase activity. The optimum KCl concentration for ATPase activity is 0.2M at pH 7.5. The activation effect of EDTA is insignificant. Thus, the smooth adductor myosin of scallop closely resembles myosins from various sources in physico-chemical properties. In enzymatic properties, however, it differs somewhat from other invertebrate myosins.
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