In:
European Journal of Biochemistry, Wiley, Vol. 137, No. 1-2 ( 1983-12), p. 95-99
Abstract:
The ATPase complex is isolated and purified from membrane vesicles of the thermophilic cyanobacterium Synechococcus 6716 by octyl glucoside and cholic acid by a modification of the procedure for its extraction from spinach chloroplasts. The complex is purified by differential centrifugation and ammonium sulfate precipitation and by gel filtration on Sepharose 6B. The purified fraction, without any phycocyanin contamination, shows ATP hydrolysis activity and P i /ATP exchange activity of 1564 and 350 nmol · min −1 · mg protein −1 , respectively. N , N′ ‐Dicyclohexylcarbodiimide inhibits the ATP hydrolysis activity of this purified fraction. On polyacrylamide gels most typical F 1 ATPase polypeptides are identified, but the low‐molecular weight polypeptides visible cannot be ascribed to the F o part of the complex with certainty; non‐identified bands around 30kDa are also present.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1983.137.issue-1-2
DOI:
10.1111/j.1432-1033.1983.tb07800.x
Language:
English
Publisher:
Wiley
Publication Date:
1983
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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