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Related Experiment Videos

Isolation and partial characterization of rat urinary esterase A2

R P McPartland, J P Rapp, M K Joseph

    Biochimica Et Biophysica Acta
    |January 12, 1983
    PubMed
    Summary

    Esterase A2, an enzyme isolated from rat urine, exhibits microheterogeneity due to sialic acid content. Its kinin-generating activity varies significantly with assay conditions, showing lower efficacy than rat urinary kallikrein.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Rat urine contains enzymes with esterase activity.
    • Esterase A2 is a specific enzyme isolated from Dahl-salt-resistant rat urine.
    • Understanding enzyme heterogeneity and activity is crucial in biochemical research.

    Purpose of the Study:

    • To isolate and characterize esterase A2 from rat urine.
    • To investigate the microheterogeneity of esterase A2.
    • To compare the kinin-generating ability of esterase A2 with rat urinary kallikrein.

    Main Methods:

    • Isolation using DEAE-Sephadex ion-exchange, aprotinin-agarose affinity, and molecular sieve chromatography.
    • Analysis of enzyme activity and heterogeneity using polyacrylamide gel electrophoresis and zymography.
    • Assessment of kinin-generating ability via bioassay and radioimmunoassay.

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    Main Results:

    • Esterase A2 preparation showed four active bands on electrophoresis, with three affected by neuraminidase treatment.
    • The enzyme preparation was free of rat urinary kallikrein.
    • Kinin-generating activity of esterase A2 was significantly lower than kallikrein, dependent on the assay method.

    Conclusions:

    • Variable sialic acid content contributes to esterase A2 microheterogeneity.
    • Esterase A2's kinin-generating potency is assay-dependent and generally less than rat urinary kallikrein.
    • Esterase A2 activity is modulated by proteins, detergents, and specific inhibitors like aprotinin and soybean trypsin inhibitor.