| Literature DB >> 2973460 |
Abstract
The alpha (62,000-dalton) and beta (49,000-dalton) subunits of Methanosarcina barkeri ATPase were purified to homogeneity. The subunits and ATPase complex were trypsinized in the presence of various nucleotides. ATP and ADP changed the trypsin sensitivity of the alpha subunit in the complex and isolated forms, suggesting the presence of a nucleotide-binding site in the alpha subunit.Entities:
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Year: 1988 PMID: 2973460 PMCID: PMC211715 DOI: 10.1128/jb.170.12.5960-5962.1988
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490