The vacuolar H(+)-translocating ATPase of renal tubules contains a 115-kDa glycosylated subunit

FEBS Lett. 1991 Apr 22;282(1):69-72. doi: 10.1016/0014-5793(91)80446-a.

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 A1, 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 of 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenal Gland Neoplasms / enzymology
  • Animals
  • Anti-Bacterial Agents / pharmacology
  • Biological Transport, Active
  • Cattle
  • Chromaffin Granules / enzymology
  • Glycosylation
  • Immunoblotting
  • Intracellular Membranes / enzymology
  • Kidney Tubules / metabolism*
  • Macrolides*
  • Microsomes / metabolism
  • Pheochromocytoma / enzymology
  • Plants / enzymology
  • Proton-Translocating ATPases / metabolism*
  • Vacuoles / enzymology*

Substances

  • Anti-Bacterial Agents
  • Macrolides
  • bafilomycin A1
  • Proton-Translocating ATPases