Abstract
The K +-stimulated phosphatase activity of microsomes from rat kidney was not inhibited by l-phenylalanine, but the HCO 3 −-stimulated phosphatase activity was markedly inhibited by l-phenylalanine. Valinomycin enhanced the HCO 3 −-stimulated phosphatase activity, but did not enhance the K +-stimulated phosphatase activity. Ouabain did not inhibit the HCO 3 −-stimulated phosphatase activity, but inhibited the K +-stimulated phosphatase activity. The renal K +-stimulated phosphatase activity was suppressed to 40% of the control values by adrenalectomy, but the renal HCO 3 −-stimulated phosphatase activity was little suppressed by adrenalectomy. The renal K +-stimulated phosphatase activity in intact and adrenalectomized rats was found to be significantly elevated, in a manner similar to the elevation of the renal (Na + + K +)-ATPase activity by aldosterone treatment ( P < 0.02).
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