Purification and Characterization of a Membrane-bound ATPase from Acetabularia cliftonii That Corresponds to a Cl-—Translocating ATPase in Acetabularia acetabulum

Chie Moritani, Toshitaka Ohhashi, Sachiko Satoh, Dieter Oesterhelt, Mikiko Ikeda

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

A Mg2+-ATPase was solubilized from membranes of Acetabularia cliftonii using nonanoyl-A-methylgluconamide and purified by ion-exchange and gel permeation chromatography. One active ATPase fraction after Mono Q chromatography had a specific activity of 10 units/mg of protein. Judged from subunit composition [54 (a), 50 (b) with a fainter band around 40 kDa], catalytic properties, and N-terminal amino acid sequence of the b subunit, the isolated enzyme was comparable to the CI-—ATPase of Acetabularia acetabulum. Immunological characterization of both subunits showed significant similarity to the F type of ATPase. CI--transport activity was observed by reconstitution studies into liposomes.

Original languageEnglish
Pages (from-to)2087-2089
Number of pages3
JournalBioscience, biotechnology, and biochemistry
Volume58
Issue number11
DOIs
Publication statusPublished - Jan 1 1994

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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