Further evidence for the existence of an intrinsic bicarbonate-stimulated Mg2+
-ATPase in brush border membranes isolated from rat kidney cortex

Kinne-Saffran, Evamaria; Kinne, Rolf

doi:10.1007/BF01871120

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Further evidence for the existence of an intrinsic bicarbonate-stimulated Mg²⁺-ATPase in brush border membranes isolated from rat kidney cortex

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Kinne-Saffran, Evamaria
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Kinne, Rolf
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Kinne-Saffran, E., & Kinne, R. (1979). Further evidence for the existence of an intrinsic bicarbonate-stimulated Mg²⁺-ATPase in brush border membranes isolated from rat kidney cortex. Journal of Membrane Biology, 49, 235-251. doi:10.1007/BF01871120.

Cite as: https://hdl.handle.net/21.11116/0000-0008-3E94-C

Abstract

The aim of this study was to provide further evidence for the existence of a nonmitochondrial bicarbonate-stimulated Mg²⁺-ATPase in brush border membranes derived from rat kidney cortex. A plasma membrane fraction rich in brush border microvilli and a mitochondrial fraction were isolated by differential centrifugation. Both fractions contain a Mg²⁺-ATPase activity which can be stimulated by bicarbonate. The two Mg²⁺-ATPases are stimulated likewise by chloride, bicarbonate, and sulfite or inhibited by oligomycin and aurovertin, though to different degrees. In contrast to these similarities, only the Mg²⁺-ATPase activity of the mitochondrial fraction is inhibited by atractyloside, a substance which blocks an adenine nucleotide translocator in the inner mitochondrial membrane. On the other hand, filipin, an antibiotic that complexes with cholesterol in the membranes inhibits exclusively the Mg²⁺-ATPase of the cholesterol-rich brush border membranes. Furthermore it could be demonstrated by the use of bromotetramisole, an inhibitor of alkaline phosphatase activity, that the Mg²⁺-ATPase activity in the membrane fraction is not due to the presence of the highly active alkaline phosphatase in these membranes. These results support the assumption that an intrinsic bicarbonate-stimulated Mg²⁺-ATPase is present in rat kidney brush border membranes.