| Literature DB >> 2879537 |
Abstract
The proton-translocating adenosine triphosphatase (ATPase) of bovine chromaffin granules contains up to five different polypeptides. Its activity is inhibited by N-ethylmaleimide, and ATP protects the enzyme from inhibition. After treatment of membranes with N-[2-3H]ethylmaleimide, only one polypeptide is strongly radiolabelled: this is the largest (70 kDa) subunit of the proton-translocating ATPase. This subunit therefore contains the ATP-hydrolysing site. Two-dimensional electrophoresis reveals heterogeneity in this polypeptide.Entities:
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Year: 1986 PMID: 2879537 PMCID: PMC1147241 DOI: 10.1042/bj2390077
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857