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Related Experiment Videos

Reactive thiol groups in rat liver acid phosphatase.

N Navaratnam, M R Banner, P J Butterworth

    Enzyme
    |January 1, 1985
    PubMed
    Summary

    Rat liver acid phosphatase P1 is inactivated by mercury compounds, but protected by substrate analogues. Fluorescein mercuriacetate (FMA) binding suggests 3-6 reactive thiol groups, with 1-2 essential per subunit.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • Dimeric rat liver acid phosphatase P1 (Mr 92,000) is a key enzyme.
    • Understanding its active site and reactive groups is crucial for enzyme function studies.

    Purpose of the Study:

    • To investigate the role of thiol groups in the activity and structure of rat liver acid phosphatase P1.
    • To determine the number and essentiality of reactive thiol groups in the enzyme.

    Main Methods:

    • Enzyme inactivation assays using p-chloromercuribenzoate and fluorescein mercuriacetate (FMA).
    • Spectrophotometric and fluorimetric monitoring of FMA-thiol reactions.
    • Statistical analysis of inactivation/modification data.

    Main Results:

    • Rat liver acid phosphatase P1 is inactivated by mercurial compounds.
    • Substrate analogue Pi protects the enzyme against inactivation.
    • FMA binding indicates 3-6 reactive thiol groups per molecule.
    • Statistical analysis suggests 1-2 essential thiol groups per subunit, with one likely at the active site.

    Conclusions:

    • Rat liver acid phosphatase P1 possesses multiple reactive thiol groups.
    • A subset of these thiol groups, potentially one per subunit, is essential for enzyme activity and located at the active site.

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