Abstract
1. Homogenates of goldfish intestinal mucosa were separated into various fractions by differential centrifugation. Both adenosine-triphosphatase and β-glycerophosphatase activities were found to be concentrated mainly in a membrane fraction which sedimented after 1200000g-min. 2. This membrane adenosine-triphosphatase system was activated by Na++K+ and inhibited by ouabain. 3. The ouabain-sensitive adenosine-triphosphatase activity was high and the ouabain-insensitive activity low in membrane fractions prepared from fish acclimatized previously to 8°. The opposite was true for fish acclimatized to 30°. 4. The Arrhenius plots of ouabain-sensitive and ouabain-insensitive adenosine-triphosphatase activities, measured from 5° to 30°, showed discontinuities at incubation temperatures that varied with the previous acclimatization temperature of the fish. 5. It is considered that modification of the membrane adenosine-triphosphatase system in goldfish intestinal mucosa may serve to regulate Na+ transport at different environmental temperatures.
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