Purification and Characterization of a Membrane-bound ATPase from<i>Acetabularia cliftonii</i>That Corresponds to a Cl<sup>−</sup>-Translocating ATPase in<i>Acetabularia acetabulum</i>

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

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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.

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