Abstract

1. 1. Cytochrome oxidase from muscle of goldfish showed an increased activity with gold acclimation and decreased activity with warm acclimation when measured at an intermediate temperature. Activity of t he enzyme from 5°C fish was three to five times greater than from 30° fish when measured 15°. 2. 2. Measurements at various temperatures showed a translation toward the left of the rate-temperature curves with cold acclination. The Q 10 over the linear range was 2·1 for enzyme preparations from fish acclimated to 5, 15, 25 or 30°. 3. 3. Enzyme activity measured at the temperatures of acclimation was maximal at 25°. 4. 4. After 2 hr of heating at 45° the cytochrome oxidase was 80 per cent inactivated, irrespective of acclimation temperature. 5. 5. After 5–10 min of heat treatment, the activity of the enzyme from 5° fish was higher than its activity without heating, decline in activity of enzyme from 15° fish was delayed, but activity from fish acclimated to 25–30° declined directly. 6. 6. It is concluded that cold acclimation causes an increase and warm acclimation a decrease in amount of cytochrome oxidase in goldfish muscle, also that in cold acclimation there is either an increase in a heat-sensitive inhibitor or a change which causes prolongation of thermal activation.

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