魚類の肉質変化に関する生化学的研究-IV : コイ筋肉の精製myosin区のATPase作用と安定性について

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In this paper, the authors dealt with the stability and ATPase activity of the purified myosin A and B fractions from carp muscle. 1) In the presence of Ca++, the maximum activity of myosin A and B fractions were observed at 30-35°C. (see Fig. 1). At 37°C. the activity was reduced within 5min. and lost completely at 45°C (see Fig. 2). Those behaviours of the myosin fractions to heat were very close to the myosin of tabit muscle. 2) The amount of free SH groups and the activity of myosin fractions was reduced when the KCl solution of myosin as stored at 25°C. Even at 0-3°C., the amount of free SH groups was reduced after the storage for 48 hours but decrease of the activity was hardly observed. It has been already pointed out that the stability of myosin increases, when ATP was present. But according to the results shown in Table 1, the activity and the amount of SH groups were markedly reduced by the addition of ATP (1×10-4Mol/L.) to the myosin fractions. The myosin fractions showed a gradual decrease of the activity when left in contact with air, and yet such preparation was treated with reducing agents such a ?? cysteine and ascorbic acid, the lost activity was not fully recovered. 3) It was observed that the flocculation of protein increased in the storage of myosin fractions, and the supernatants after centrifugation of such preparations showed to gradually decrease in the amount of nitrogen, the relative viscosity and the activity. And myosin fractions were rapidly denatured even at temperatcre below 40°C.

魚類の肉質変化に関する生化学的研究-IV : コイ筋肉の精製myosin区のATPase作用と安定性について

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