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PMID: 135756 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Properties of Escherichia coli mutants with alterations in Mg2+-adenosine triphosphatase.

Journal of bacteriology ·Vol. 128 ·No. 1 ·1976-10-00 ·Pages 248-56

Adler LW, Rosen BP

Abstract

A mutant Escherichia coli, selected for resistance to the antibiotic neomycin, was unable to utilize nonfermentable carbon sources for growth. Two strains were selected from this mutant on the basis of their ability to grow utilizing succinate as a carbon source. All three strains had approximately equal amounts of the Mg2+-adenosine triphosphatase (ATPase) (EC 3.6.1.3) protein, but the activity of the enzyme differed in each strain. The Mg2+-ATPase from each of the three strains lost activity upon solubilization and appeared to undergo rapid dissociation once solubilized. This dissociation is similar to that described for the wild type after cold exposure.

MeSH Terms
Adenosine Triphosphatases/analysis,isolation & purification,metabolism Cell Membrane/metabolism Chromosome Mapping Chromosomes, Bacterial Dicyclohexylcarbodiimide/pharmacology Drug Resistance, Microbial Escherichia coli/enzymology,metabolism Ethanol/pharmacology Immunodiffusion Immunoelectrophoresis Mutation Neomycin/pharmacology
Chemicals
Ethanol Dicyclohexylcarbodiimide Adenosine Triphosphatases Neomycin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Adler L W
Rosen B P
References (18)
18 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1976-10-00
Pages
248-56
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC232850
Subset
IM
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