Abstract
In this paper the authors dealt with the AMPdeaminase activity of some fractions extracted from carp and mackerel muscle. The results obtained were as follows: 1) AMPdeaminase activity was similarly found in both actomyosin fraction and water extract II fraction which prepared by KALCKAR's method, while ATPase activity was not observed in the latter. 2) The enzymic characteristics of AMPdeaminase activity (such as opt. pH and opt. temp.) was found to be almost identical in both fractions. The optimum pH of the activity lay at pH 6.5, the optimum temperature being 38°C. The activity was not lost completely even by exposene to 50°C. for 30 minutes. At the concentration of 0.01-0.001 mol/l Ca++ and Mg++ showed no effect on the enzymic action, but Cu++ and Ag+ inhibited the activity even in very low concentration. 3) In case of the fish muscle kept at 25°C., it was observed that AMPdeaminase activity of water extract II fraction increased with time so far as the experiment was concerned (from 5 to 12 hours after its death). On the basis of some experimental evidences, it was suggested that ammonia accumulation during autolysis was caused, at least in part, by deamination of AMP.
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