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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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Bibliografski detalji
Glavni autori: Hicks, D B, Krulwich, T A
Format: Artigo
Jezik:Inglês
Izdano: 1987
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC213849/
https://ncbi.nlm.nih.gov/pubmed/2888751
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