These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: F0F1-ATPase from Vibrio alginolyticus. Subunit composition and proton pumping activity.
    Author: Dmitriev OYu, Krasnoselskaya IA, Papa S, Skulachev VP.
    Journal: FEBS Lett; 1991 Jun 24; 284(2):273-6. PubMed ID: 1647986.
    Abstract:
    An F0F1-ATPase was isolated from the membranes of the marine bacterium Vibrio alginolyticus. Homology between the subunits of the F0-complexes from E. coli and V. alginolyticus was found using antibodies against subunits a, b and c of the E. coli F0F1-ATPase. The F0F1-complex from V. alginolyticus was reconstituted into proteoliposomes, which were competent in ATP-dependent proton uptake. This process was inhibited by triphenyltin, DCCD, and venturicidin. Na+ did not affect proton translocation.
    [Abstract] [Full Text] [Related] [New Search]