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Related Experiment Videos

Specific method for the purification of Streptococcus mutans dextransucrase

M M McCabe, E E Smith

    Infection and Immunity
    |June 1, 1977
    PubMed
    Summary
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    Purifying Streptococcus mutans dextransucrase is now easier. This method uses affinity and hydrophobic chromatography for over 1,000-fold purification, yielding two enzyme components with distinct properties.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Enzymology

    Background:

    • Streptococcus mutans dextransucrase is crucial for dental plaque formation.
    • Efficient purification methods are needed to study enzyme function and inhibition.

    Purpose of the Study:

    • To develop a rapid and effective purification protocol for Streptococcus mutans dextransucrase.
    • To characterize the purified enzyme components and their catalytic activities.

    Main Methods:

    • Affinity chromatography using insoluble dextran.
    • Hydrophobic interaction chromatography on butyl-agarose.

    Main Results:

    • Achieved over 1,000-fold purification of dextransucrase with 65% activity recovery.
    • Separated two distinct dextransucrase components.

    Related Experiment Videos

  • Identified differential stimulation of enzyme activity by exogenous soluble dextran.

    • Conclusions:

    • The developed method provides highly purified Streptococcus mutans dextransucrase.
    • Two enzyme components exhibit different regulatory properties, impacting glucan synthesis.