TY - JOUR
T1 - Purification and Characterization of a Membrane-bound ATPase from Acetabularia cliftonii That Corresponds to a Cl-—Translocating ATPase in Acetabularia acetabulum
AU - Moritani, Chie
AU - Ohhashi, Toshitaka
AU - Satoh, Sachiko
AU - Oesterhelt, Dieter
AU - Ikeda, Mikiko
N1 - Funding Information:
Acknowledgments. We are grateful to Professor Dr. Traub of the Max-Planck-Institute of Cell Biology, for supplying cells of A. eliftonii, and to Dr. K. Inagaki of the University of Okayama for operating a protein/peptide sequencer. Thanks are extended to Professor Dr. K. Altendorf of the University of Osnabrueck for supplying the antisera against the IJ. and f3 subunits of E. coli F l-ATPase, to Dr. Y. Tomita and Dr. T. Tsuchiya of the University of Okayama for supplying the antisera against V. parahaemolYlicus ATPase, to Dr. Y. Mukohata of the University of Nagoya for supplying the anti-IgG fractions of H. halobium ATPase, and to Dr. M. Maeshima of the Institute of Low Temperature Science of the University of Hokkaido for supplying the antibodies against mung bean vacuolar ATPase. This work was in part supported by a grant under the Monbusho International Scientific Research Program (No. 02044101 and No. 04044123), bya grant from the Takeda Science Promotion Society, and by a grant from the Hayashi Memorial Foundation for Female Natural Scientists.
PY - 1994
Y1 - 1994
N2 - 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.
AB - 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.
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U2 - 10.1271/bbb.58.2087
DO - 10.1271/bbb.58.2087
M3 - Article
C2 - 7765601
AN - SCOPUS:0028545177
SN - 0916-8451
VL - 58
SP - 2087
EP - 2089
JO - Bioscience, biotechnology, and biochemistry
JF - Bioscience, biotechnology, and biochemistry
IS - 11
ER -