Literature DB >> 2532151

The F1-ATPase of Vibrio alginolyticus. Purification and N-terminal sequence of major subunits.

V A Grinkevich, V P Skulachev.   

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.

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Year:  1989        PMID: 2532151     DOI: 10.1016/0014-5793(89)81657-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Kinetic models of coupling between H+ and Na(+)-translocation and ATP synthesis/hydrolysis by F0F1-ATPases: can a cell utilize both delta mu H+ and delta mu Na+ for ATP synthesis under in vivo conditions using the same enzyme?

Authors:  B N Kholodenko
Journal:  J Bioenerg Biomembr       Date:  1993-06       Impact factor: 2.945

2.  Characterization of a membrane-associated ATPase from Methanococcus voltae, a methanogenic member of the Archaea.

Authors:  W Chen; J Konisky
Journal:  J Bacteriol       Date:  1993-09       Impact factor: 3.490

3.  Characterization of the H(+)-pumping F1F0 ATPase of Vibrio alginolyticus.

Authors:  L R Krumholz; U Esser; R D Simoni
Journal:  J Bacteriol       Date:  1990-12       Impact factor: 3.490

4.  Catabolite repression of the H(+)-translocating ATPase in Vibrio parahaemolyticus.

Authors:  Y Sakai-Tomita; C Moritani; H Kanazawa; M Tsuda; T Tsuchiya
Journal:  J Bacteriol       Date:  1992-11       Impact factor: 3.490

  4 in total

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