Abstract
A Mg2+-ATPase was solubilized from membranes of Acetabularia 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 40 kDa], 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.
| 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 - 1994 |
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ASJC Scopus subject areas
- Biotechnology
- Molecular Biology
- Biochemistry
- Organic Chemistry
- Analytical Chemistry
- Applied Microbiology and Biotechnology
- Food Science
- Biochemistry, Genetics and Molecular Biology(all)
- Chemistry (miscellaneous)
Cite this
Purification and characterization of a membrane-bound atpase from acetabularia cliftonii that corresponds to a cl--Translocating ATPase in A cetabularia acetabulum. / Moritani, Chie; Oohashi, Toshitaka; Satoh, Sachiko; Oesterhelt, Dieter; Ikeda, Mikiko.
In: Bioscience, Biotechnology and Biochemistry, Vol. 58, No. 11, 1994, p. 2087-2089.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and characterization of a membrane-bound atpase from acetabularia cliftonii that corresponds to a cl--Translocating ATPase in A cetabularia acetabulum
AU - Moritani, Chie
AU - Oohashi, Toshitaka
AU - Satoh, Sachiko
AU - Oesterhelt, Dieter
AU - Ikeda, Mikiko
PY - 1994
Y1 - 1994
N2 - A Mg2+-ATPase was solubilized from membranes of Acetabularia 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 40 kDa], 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.
AB - A Mg2+-ATPase was solubilized from membranes of Acetabularia 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 40 kDa], 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.
UR - http://www.scopus.com/inward/record.url?scp=0028545177&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028545177&partnerID=8YFLogxK
U2 - 10.1080/bbb.58.2087
DO - 10.1080/bbb.58.2087
M3 - Article
C2 - 7765601
AN - SCOPUS:0028545177
VL - 58
SP - 2087
EP - 2089
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 11
ER -