Purification and Characterization of a Membrane-bound ATPase from Acetabularia clifeonii That Corresponds to a Cl^- -Translocating ATPase in Acetabularia acetabulum
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概要
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A Mg^<2+>-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.
- 社団法人日本農芸化学会の論文
- 1994-11-23
著者
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Ikeda M
Fujisaki Institute Hayashibara Biochemical Laboratories Inc.
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SHEN Shihua
Institute of Biological Sciences, University of Tsukuba
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Satoh S
Tohoku Univ. Sendai Jpn
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Satoh S
Institute Of Biological Sciences University Of Tsukuba
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Shen Shihua
Gene Research Center University Of Tsukuba
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Ikeda M
Kyoto Pharmaceutical Univ. Kyoto Jpn
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Moritani Chie
Faculity Of Medicine Okayama University
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Ohhashi Toshitaka
Department of Molecular Biology and Biochemistry, Okayama University Medical School
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Satoh Sachiko
Research Institute of Technology, Okayama University of Science
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Oesterhelt Dieter
Max-Planck-Institute of Biochemistry
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Ikeda Mikiko
Faculty of Health and Welfare Science, Okayama Prefectural University
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Ikeda Masao
Fujisaki Institute Hayashibara Biochemical Laboratories Inc.
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Ohhashi Toshitaka
Faculity Of Medicine Okayama University
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