The K+- and HCO3−-stimulated phosphatase activities in renal microsomes of rats |
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| Institution: | Shizuoka College of Pharmacy, Department of Environmental Biochemistry, 2-2-1 Oshika, Shizuoka 422, Japan |
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| Abstract: | The K+-stimulated phosphatase activity of microsomes from rat kidney was not inhibited by l-phenylalanine, but the HCO3?-stimulated phosphatase activity was markedly inhibited by l-phenylalanine. Valinomycin enhanced the HCO3?-stimulated phosphatase activity, but did not enhance the K+-stimulated phosphatase activity. Ouabain did not inhibit the HCO3?-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 HCO3?-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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| Keywords: | Phosphatase Adrenal regulation (Rat kidney microsome) |
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