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. 1981 Oct;148(1):257–264. doi: 10.1128/jb.148.1.257-264.1981

Isolation of IIIGlc of the phosphoenolpyruvate-dependent glucose phosphotransferase system of Salmonella typhimurium.

B J Scholte, A R Schuitema, P W Postma
PMCID: PMC216188  PMID: 7026533

Abstract

We report a procedure for the isolation of IIIglc of Salmonella typhimurium, a protein component of the phosphoenolpyruvate-dependent sugar phosphotransferase system. IIIGlc is a soluble protein with a molecular weight of 21,000, as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified protein is involved in the phosphoenolpyruvate-dependent phosphorylation of methyl alpha-glucoside in vitro. Its affinity for octyl-Sepharose may be an indication of the partial hydrophobic nature of IIIGlc. A specific antiserum against purified IIIGlc was prepared. Growth on different carbon sources did not affect the synthesis of IIIGlc, as determined by quantitative immunoelectrophoresis. Mutations which lower the adenosine 3',5'-phosphate level, such as cya and pts, do not alter the IIIGlc level. The closely related enteric bacteria Escherichia coli and Klebsiella aerogenes contain a protein factor which is closely related to IIIGlc of S. typhimurium, whereas Staphylococcus aureus does not.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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