By Felix Bronner, Arnost Kleinzeller (Eds.)

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It was originally thought that this complex must be of very low energy and could represent a partial reversal (through ouabain “induction”), of the reaction sequence. Subsequent results suggested that this interpretation is too simple. The electrophoretic patterns of the E-P-”P previously digested by peptic or Pronase treatments, were examined. Profiles of E-PJ2P formed from ATP-32P and Pi-32P(the latter formed in the presence of ouabain) , were identical. Some experiments employed p h o ~ p h a t e - ~and ~ P -33Pprecursors; profiles of the mixture yielded common patterns.

C. K+-Phosphatase Judah and his colleagues (1962a; Ahmed and Judah, 1964) reported that membrane preparations contain a system that catalyzes the hydrolysis of p-nitrophenylphosphate (PNPP) in the presence of potassium. , 1966) found that this potassiumphosphatase (K+-Pase) had a similar subcellular distribution to Na+ , K+ATPase. Treatment with NaI increased the activity of both, and ouabain, protarnine, p-chloromereuribenzoate, igrosin, and acetone inhibited both activities. Potassium could be replaced by rubidium, ammonium, and cesium; lithium had little effect.

The authors suggested this series of possible complex formations: E + ATP S E - ATP + K+ K+ - E K+ - E + ATPSK’ - E - ATP E E-ATP+K+eK+-E-ATP Brodsky and Shamoo (1971) suggested that the complex formed between ATP and the “microsomal” protein resembles that expected of a phosphoramido bond. Although this hypothesis is provocative, the data supporting it are scanty and rely chiefly on pH profile. It should be emphasized that the protocols of the experiments by Shamoo and Brodsky (1972) and the studies by NGrby and Jensen (1971) are different, but both results suggest an intermediary membrane-ATP complex.

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