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

概要

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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. (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. (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. (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. (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. (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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