Purification and characterization of the F1 ATPase from Bacillus subtilis and its uncoupler-resistant mutant derivatives.

The F1 ATPase of Bacillus subtilis BD99 was extracted from everted membrane vesicles by low-ionic-strength treatment and purified by DEAE-cellulose chromatography, hydrophobic interaction chromatography, and anion-exchange high-performance liquid chromatography. The subunit structure of the enzyme w...

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Pubblicato in:	J Bacteriol
Autori principali:	Hicks, D B, Krulwich, T A
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	American Society for Microbiology (ASM) 1987
Soggetti:	Research Article
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC213849/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2888751/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.169.10.4743-4749.1987
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