魚類の肉質変化に関する生化学的研究-IIIコイ筋肉精製 myosin 区のATPase 作用

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In this paper, the authors dealt with the some enzymic properties of purified myo in A and B fractions obtained from carp muscle. The myosin A fraction was extracted from the muscle tissue by a short-time extraction for some 15 to 20min. and B fraction was obtained by the extraction for 24 hours. 1) The sufficient amount of myosin preparation was able to libera ?? e about one-half of the ?? 7P from ATP in a prolonged incubation at 37°C. 2) In the presence of Ca++, the pH-activity curve obtained showed a peculiar shape with two maxima (see Fig. 2). The maximum activities of myosin A and B fraction were obtained at about pH 9.0. 3) The influence of several ions and urea at 2.2×10-3 Mol/L. to the ATPase activity was studied, and the results were listed in Table 1. Ca++ and Mn++ ions activated the enzyme and the activation was most marked in the case of Ca++. On the contrary, Mg++ had no activating effect, but showed a marked inhibitory effect to the system activated by Ca++. At the above concentration, Fe+++ and urea showed no effect on the enzymic action. Cu++ and Ag+ retarded the ATPase action completely, even in very low concentration. 4) The nature of enzymic activity was found to be almost same in both fractions.
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