This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Scholte, B J Articles by Postma, P W Search for Related Content PubMed PubMed Citation Articles by Scholte, B J Articles by Postma, P W

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

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.

This article has been cited by other articles:

• Leydesdorff, L., Amsterdamska, O. (1990). Dimensions of Citation Analysis. Science Technology Human Values 15: 305-335 [Abstract]  
• Rohwer, J. M., Meadow, N. D., Roseman, S., Westerhoff, H. V., Postma, P. W. (2000). Understanding Glucose Transport by the Bacterial Phosphoenolpyruvate:Glycose Phosphotransferase System on the Basis of Kinetic Measurements in Vitro. J. Biol. Chem. 275: 34909-34921 [Abstract] [Full Text]