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

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

A Mg2+-ATPase was solubilized from membranes of Acetabular-ia cliftonii using nonanoyl-N-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 com...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry Vol. 58; no. 11; p. 2087
Main Authors: Moritani, Chie, Ohhashi, Toshitaka, Satoh, Sachiko, Oesterhelt, Dieter, Ikeda, Mikiko
Format: Journal Article
Language:English
Published: Tokyo Oxford University Press 01-11-1994
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Summary:A Mg2+-ATPase was solubilized from membranes of Acetabular-ia cliftonii using nonanoyl-N-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 40kDa], catalytic properties, and N-terminal amino acid sequence of the b subunit, the isolated enzyme was comparable to the Cl- -ATPase of Acetabularia acetabulum. Immunological characterization of both subunits showed significant similarity to the F type of ATPase. Cl- -transport activity was observed by reconstitution studies into liposomes.
ISSN:0916-8451
1347-6947