The vacuolar H+‐translocating ATPase of renal tubules contains a 115‐kDa glycosylated subunit

FEBS Letters

Warren, Mark¹  Haywood, Jeff¹  Gillespie, John¹  Ozanne, Susan¹  Percy, Judith¹  Apps, David¹ 

[1] Department of Biochemistry, University of Edinburg, Edinburgh, UK

关键词: Kidney;    Proton translocation;    ATPase;    Glycoprotein;   

DOI  :  10.1016/0014-5793(91)80446-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown