抄録
The stability of black marlin and jack mackerel myosins and their fragments to high hydrostatic pressure (100, 200, 300, 400, and 500 MPa) was examined by meansof a solubility test, CD measurement, and changes in fluorescence intensity. The solubility of both myosins decreased with the hydrostatic pressure-treatment above 300 MPa. There was a marked decrease in thesolubility of S-1, especially in the presence of 0.05M KCl, though the solubility of rod did not alter. The results of CD measurements showed a slight decrease in the helical content of myosins and S-1s. From the data of binding of ANS (8-anilino-1-naphthalene sulfonate), it was indicated that by pressure treatment the fluorescence intensities of myosins and S-ls increased rapidly. By the changes of tryptophan fluorescence intensity the pressure-treated S-1s in 0.05M KCl showed rapidly decreasing curves. The pressure-stability of S-1s in 0.05M KCl was very inferior to that of S-1s in 0.6M KCl.
