title: The F1-ATPase of Vibrio alginolyticus. Purification and N-terminal sequence of major subunits.
abstract: The F1-type ATPase has been isolated from membrane preparations of marine alkalotolerant bacterium, Vibrio alginolyticus. The enzyme was found to consist of two major subunits of 55 and 58 kDa and at least two minor components (38 and 23 kDa). Amino acid sequences of N-terminal regions of the major subunits revealed close homology with those of E. coli H+-ATPase and of Propionigenium modestum Na+-ATPase.
authors.affiliation: A.N. Belozersky Laboratory for Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
authors.lastname: Dmitriev OYu
authors.forename: V A
authors.initials: VA
authors.lastname: Grinkevich
authors.forename: V P
authors.initials: VP
authors.lastname: Skulachev
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000201:enzymology; D002852:Chromatography, Ion Exchange; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000302:isolation & purification* / Q000378:metabolism; D014733:Vibrio / Q000201:enzymology*
chemical_list: D046911:Macromolecular Substances; D004024:Dicyclohexylcarbodiimide; D006180:Proton-Translocating ATPases