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The vacuolar H + ‐translocating ATPase of renal tubules contains a 115‐kDa glycosylated subunit
Author(s) -
Gillespie John,
Ozanne Susan,
Percy Judith,
Warren Mark,
Haywood Jeff,
Apps David
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80446-a
Subject(s) - protein subunit , atpase , bafilomycin , biochemistry , molecular mass , microsome , vacuole , biology , chemistry , kidney , v atpase , microbiology and biotechnology , enzyme , endocrinology , cytoplasm , apoptosis , autophagy , gene
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.