PURIFICATION AND CHARACTERIZATION OF THE F1 PORTION OF THE ATP SYNTHASE (F1F0) OF STREPTOMYCES-LIVIDANS

Autor(en): HENSEL, M 
DECKERSHEBESTREIT, G
ALTENDORF, K 
Stichwörter: Biochemistry & Molecular Biology; CHLOROPLASTS; ESCHERICHIA-COLI; F1-ATPASE; H+; MEMBRANE ATPASE; MITOCHONDRIA; POLYACRYLAMIDE-GEL ELECTROPHORESIS; RECONSTITUTION; SUBUNIT; THERMOPHILIC BACTERIUM PS3
Erscheinungsdatum: 1991
Herausgeber: WILEY
Enthalten in: EUROPEAN JOURNAL OF BIOCHEMISTRY
Band: 202
Ausgabe: 3
Startseite: 1313
Seitenende: 1319
Zusammenfassung: 
The F1 complex of the ATP synthase of Streptomyces lividans was isolated and purified. The procedure involved the solubilization of F1 from membranes with buffer of low ionic strength in the presence of EDTA, ion-exchange chromatography and gel filtration. The purified F1 complex from S. lividans (SLF1) consists of five subunits alpha, beta, gamma, delta and epsilon with molecular masses of 58 000, 50 000, 36 000, 28 000 and 13 000, respectively and exhibits immunological cross-reactivity with the F1 portion purified from Escherichia coli (ECF1). The enzymatic properties of SLF1 were determined by the use of microtiter-plate-based assay and compared with data obtained for ECF1. ATPase activity of SLF1 (specific activity: 20-30 U/mg) was only observed in the presence of high concentrations of Ca2+ (10 mM). Stimulation of the ATPase activity by Mg2+ was not detectable; quite to the contrary, Mg2+ inhibited the Ca2+-stimulated activity of SLF1. SLF1 was re-bound to F1-stripped membranes of S. lividans, but not to F1-stripped membrane vesicles of E. coli. In contrast, ECF1 could be cross-reconstituted with F1-stripped membranes of S. lividans; however, a structural but not a functional reconstitution of the hybrid F1F(o) complex was observed.
ISSN: 00142956
DOI: 10.1111/j.1432-1033.1991.tb16505.x

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