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    Identification of methionine-processed HPr in the equine pathogen Streptococcus equi

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    Publication date
    2000-10
    Author
    Sutcliffe, I.C.
    Trigg, J.
    Harrington, Dean J.
    Keyword
    HPr; Strangles; Streptococcus
    Peer-Reviewed
    Yes
    
    Metadata
    Show full item record
    Abstract
    Using 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.
    URI
    http://hdl.handle.net/10454/11591
    Version
    No full-text in the repository
    Citation
    Sutcliffe 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.
    Link to publisher’s version
    http://dx.doi.org/10.1016/S0723-2020(00)80061-2
    Type
    Article
    Collections
    Life Sciences Publications

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