Literature DB >> 2889695

Immunochemical evidence for an active (F1-F0)-ATPase in mycoplasmas.

S Rottem1, M H Shirvan, M F Barile, D Zilberstein.   

Abstract

In all Acholeplasma, Mycoplasma and Spiroplasma species tested, a protein capable of reacting with antibodies prepared against the beta subunit of the proton-ATPase complex from yeast, chloroplasts and Escherichia coli was detected. The reactive protein of M. gallisepticum was found to be catalytically active, suggesting that mycoplasmas, as other bacteria, possess a proton-translocating ATPase. Characterization of the ATPase activity of M. gallisepticum indicates that this organism also possesses a Na+-stimulated ATPase activity that differs from the proton-ATPase in its pH profile and its resistance to dicyclohexylcarbodiimide (DCCD).

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Year:  1987        PMID: 2889695

Source DB:  PubMed          Journal:  Isr J Med Sci        ISSN: 0021-2180


  2 in total

1.  Nucleotide sequence, organization and characterization of the atp genes and the encoded subunits of Mycoplasma gallisepticum ATPase.

Authors:  O F Rasmussen; M H Shirvan; H Margalit; C Christiansen; S Rottem
Journal:  Biochem J       Date:  1992-08-01       Impact factor: 3.857

2.  Volume regulation in Mycoplasma gallisepticum: evidence that Na+ is extruded via a primary Na+ pump.

Authors:  M H Shirvan; S Schuldiner; S Rottem
Journal:  J Bacteriol       Date:  1989-08       Impact factor: 3.490

  2 in total

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