Abstract
Drapeau, Gabriel R., (Macdonald College of McGill University, Quebec, Canada) and Robert A. MacLeod. Nutrition and metabolism of marine bacteria. XII. Ion activation of adenosine triphosphatase in membranes of marine bacterial cells. J. Bacteriol. 85:1413–1419. 1963.—Isolated membranes of two species of marine bacteria, a Pseudomonas and a Cytophaga, have been shown to possess adenosine triphosphatase activity. The optimal pH for enzyme action of both organisms was 8.8. The enzyme system was found to be capable of splitting inorganic o-phosphate from adenosine triphosphate (ATP), adenosine diphosphate, adenosine monophosphate, and inosine triphosphate but not from inorganic pyrophosphate. Mg++ was required for enzyme activity; with the Pseudomonas species, the optimal Mg++ to ATP ratio was 1:1. Ca++ could not replace Mg++. In the presence of the optimal concentration of Mg++, the enzyme system was further stimulated, nonspecifically, by a number of different salts. Maximal activation was achieved at an ionic strength of 0.3 to 0.4. No evidence of an adenosine triphosphatase specifically activated by a combination of Na+ and K+ was obtained with either organism. No effect of ouabain on either the membrane adenosine triphosphatase activity or Na+ transport by whole cells could be detected. The results suggest that the mechanism of ion regulation in marine bacterial cells is different from that in animal cells.
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