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 language | English |
|---|---|
| Pages (from-to) | 2087-2089 |
| Number of pages | 3 |
| Journal | Bioscience, biotechnology, and biochemistry |
| Volume | 58 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Jan 1 1994 |
ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry
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Moritani, C., Ohhashi, T., Satoh, S., Oesterhelt, D., & Ikeda, M. (1994). Purification and Characterization of a Membrane-bound ATPase from Acetabularia cliftonii That Corresponds to a Cl-—Translocating ATPase in Acetabularia acetabulum. Bioscience, biotechnology, and biochemistry, 58(11), 2087-2089. https://doi.org/10.1271/bbb.58.2087