title: Characterization of a P-type ATPase of the archaebacterium Methanococcus voltae.
abstract: The vanadate-sensitive ATPase of Methanococcus voltae has been purified by a procedure which includes, purification of the cytoplasmic membrane by sucrose gradient centrifugation, solubilization with Triton X-100, and DEAE-Sephadex and Sephacryl S-300 chromatography. While the DEAE-Sephadex step provided a preparation consisting of two polypeptides (74 and 52 kDa), the Sephacryl S-300 step yields a product with a subunit of 74 kDa. Incubation of either membranes or purified ATPase with [gamma-32P]ATP followed by acidic (pH 2.4) lithium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated the vanadate-sensitive labeling of a 74-kDa acyl phosphate intermediate. These results indicate that the M. voltae ATPase is of the P-type.
authors.affiliation: Department of Microbiology, University of Illinois, Urbana 61801.
authors.forename: R M
authors.initials: RM
authors.lastname: Dharmavaram
authors.forename: J
authors.initials: J
authors.lastname: Konisky
mesh_terms: D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000900:Anti-Bacterial Agents; D001105:Archaea / Q000187:drug effects / Q000201:enzymology; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D019605:Euryarchaeota / Q000187:drug effects / Q000201:enzymology*; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins / Q000494:pharmacology; D007783:Lactones / Q000494:pharmacology; D018942:Macrolides; D009573:Nitrites / Q000494:pharmacology; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D013861:Thiocyanates / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D005452:Fluoresceins; D007783:Lactones; D018942:Macrolides; D009573:Nitrites; D010750:Phosphoproteins; D013861:Thiocyanates; C040929:bafilomycin A1; D000251:Adenosine Triphosphatases; D016650:Fluorescein-5-isothiocyanate