Abstract
Kidney microsomes were fractionated with Triton X-114, to give a fraction enriched in the renal tubule H +-translocating ATPase, as judged by the sensitivity of its ATPase activity to bafilomycin A 1, and its content of two polypeptides recognized by antibodies directed against subunits of plant tonoplast ATPases. This fraction contained a polypeptide of apparent molecular mass of 115 kDa, that was recognized by an antibody to the largest (120 kDa) subunit chromaffin-granule membrane H +-ATPase, and, like this subunit, was reduced in molecular weight on treatment with glycopeptidase F. We conclude that, like other mammalian vacuolar H +-ATPases, the kidney H +-ATPase contains a large, glycosylated subunit.
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