Abstract
Myosin was extracted from the ordinary muscle of requiem shark Triakis scyllia by a high ionic strength extractant containing ATP, and purified by fractionation with ammonium sulfate and EDAE-cellulose column chromatography. Requiem shark myosin thus purified was found to be homogeneous by ultracentrifugal and electrophoretical measurements. The sedimentation constant (s020, w) of this myosin was 6.7 S. Subunit molecular weights, as estimated by SDS-gel electrophoresis, were 200, 000 for heavy chain, 25, 000 for A1 light chain, 17, 5000 for DTNB light chain, and 14, 000 for A2 light chain. The molar ratio of A1 to A2 light chain was determined to be 2.6. The amino acid composition of requiem shark myosin featured higher lysine and glutamic acid contents and lower aspartic acid valine contents, compared to those of other myosins. The inactivation rate constant was 2.4×10-3 s-1 at 30°C, when Ca2+-ATPase activity was used as a parameter.
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