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Purification of Streptococcus faecium penicillin binding protein 5, a multifunctional penicillin-binding protein

A Grossato, Y R Cheng, E Tonin

    Microbiologica
    |January 1, 1986
    PubMed

    Insights

    Researchers purified penicillin-binding protein 5 from Streptococcus faecium using affinity chromatography and gel electrophoresis. This method successfully isolated the protein while preserving its native properties for further study.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Protein Chemistry

    Background:

    • Penicillin-binding protein 5 (PBP 5) is a crucial enzyme in Streptococcus faecium.
    • Understanding PBP 5's function requires isolating it from complex membrane structures.

    Purpose of the Study:

    • To develop a method for purifying Streptococcus faecium PBP 5.
    • To ensure the purified protein retains its native functional properties.

    Main Methods:

    • Solubilization of membrane proteins.
    • Covalent affinity chromatography for partial separation.
    • SDS-polyacrylamide gel electrophoresis for homogeneity.
    • Elution and renaturation to restore activity.

    Main Results:

    • Penicillin-binding protein 5 was successfully solubilized and purified to homogeneity.
    • The purification process preserved the protein's essential characteristics observed in its native membrane environment.
    • The isolated PBP 5 retained its penicillin-binding activity.

    Conclusions:

    • A robust purification protocol for Streptococcus faecium PBP 5 has been established.
    • The method allows for the isolation of functional PBP 5, suitable for detailed biochemical and structural analysis.
    • This facilitates further research into PBP 5's role in bacterial cell wall synthesis and antibiotic resistance.

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