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Related Experiment Videos

Uricase from fish liver: isolation and some properties.

J E Kinsella, B German, J Shetty

    Comparative Biochemistry and Physiology. B, Comparative Biochemistry
    |January 1, 1985
    PubMed
    Summary

    This study quantifies uricase activity in fish livers, revealing significant variations. Lake trout uricase was purified, characterized, and found to be an oligomeric enzyme with optimal activity at pH 8.8.

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    Area of Science:

    • Biochemistry
    • Comparative Physiology
    • Enzymology

    Background:

    • Uricase (urate: oxygen oxidoreducase EC.1.7.3.3) is a key enzyme in purine metabolism.
    • Understanding uricase activity across different fish species is important for comparative biochemistry.

    Purpose of the Study:

    • To measure and compare uricase activities in the livers of various fish species.
    • To purify and characterize the uricase enzyme from lake trout.

    Main Methods:

    • Enzyme activity assays were performed on liver homogenates from rainbow trout, mackerel, lake trout, catfish, shark, and tilapia.
    • Lake trout uricase was purified using ammonium sulfate precipitation, protamine sulfate treatment, and Sephacryl S-200 chromatography.
    • Enzyme properties including subunit size, pH optimum, Km, and Vmax were determined using SDS-PAGE and kinetic assays.

    Main Results:

    • Uricase activities varied significantly among species, with mackerel (1180 units/g) and rainbow trout (1000 units/g) showing the highest levels.
    • Lake trout uricase was purified 20-fold and identified as an oligomeric enzyme with 32,500-dalton subunits.
    • The enzyme exhibited optimal activity at pH 8.8, with a broad activity range from pH 7.0 to 9.5, and apparent Km and Vmax values of 80 µM and >1000 units, respectively.

    Conclusions:

    • Significant interspecies variation in fish liver uricase activity exists.
    • Lake trout liver uricase is a well-characterized oligomeric enzyme with specific kinetic properties and pH optima.

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