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dc.contributor.authorSutcliffe, I.C.*
dc.contributor.authorTrigg, J.*
dc.contributor.authorHarrington, Dean J.*
dc.date.accessioned2017-03-10T15:55:34Z
dc.date.available2017-03-10T15:55:34Z
dc.date.issued2000-10
dc.identifier.citationSutcliffe IC, Trigg J and Harrington DJ (2000) Identification of methionine-processed HPr in the equine pathogen Streptococcus equi. Systematic and Applied Microbiology. 23(3): 330-332.en_US
dc.identifier.urihttp://hdl.handle.net/10454/11591
dc.descriptionNoen_US
dc.description.abstractUsing preparative electrophoresis, a low molecular weight protein has been partially purified from a cell extract of the equine pathogen Streptococcus equi susp. equi. N-terminal sequence analysis and Western blotting revealed the protein to be HPr, a central component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). Interestingly, the only form of the HPr protein detected in S. equi was one with the amino-terminal methionine removed, a modification that has previously been associated with surface localization of streptococcal HPr proteins.en_US
dc.language.isoenen_US
dc.subjectHPr; Strangles; Streptococcusen_US
dc.titleIdentification of methionine-processed HPr in the equine pathogen Streptococcus equien_US
dc.status.refereedYesen_US
dc.typeArticleen_US
dc.type.versionNo full-text in the repositoryen_US
dc.identifier.doihttps://doi.org/10.1016/S0723-2020(00)80061-2


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