Preparation and Biochemical Properties of Subfragment-1 from Dorsal Muscle of Carp <i>Cyprinus carpio</i>

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  • IKARIYA Toshinori
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University
  • KIMURA Ikuo
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University
  • ARAI Ken-ichi
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University

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  • コイ背肉ミオシンからサブフラグメント‐１の調製とその生化学的性質について
  • コイ セニク ミオシン カラ サブフラグメントー1 ノ チョウセイ ト ソノ

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A method was developed to obtain subfragment-1 (S-1) from carp dorsal muscle myosin by chymotryptic digestion. The biochemical properties of carp S-1 were studied.<br> (1) Carp myosin was more highly sensitive to chymotryptic digestion than was rabbit myosin. The digestion at 10°C instead of 20°C was therefore preferable to obtain the biologically active fragment from carp myosin.<br> (2) The carp S-1 was shown to be homogeneous on gel filtration-gel electrophoresis, and on ultracentrifugation. The sedimentation constant was estimated to be 5.38 S (2.6 mg/ml), which was comparable to rabbit S-1.<br> (3) The SDS-gel electrophoretic patterns showed that carp S-1 contained two light chains of different molecular weights, but the smallest light chain of myosin was lost during chymotryptic digestion.<br> (4) The ATPase activity of carp S-1 was found to be very similar to that of rabbit S-1 in the following repects: KCl concentration dependence, pH dependence, and kinetic parameters (Vmax and Ka) in actin activation.<br> (5) The plots of the changes in light scattering intensity and turbidity of carp S-1 against F-actin concentration indicated that one mole of S-1 (estimated M.W.: 1.0×105) was bound per mole of actin monomer.

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