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Mouse kidney trehalase: purification and properties.

M N Tenan, C P de Oliveira, A D Panek

    Anais Da Academia Brasileira De Ciencias
    |March 1, 1979
    PubMed
    Summary
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    Researchers purified mouse kidney trehalase (E.C.3.2.1.28), a specific enzyme. This study details its properties, including optimal conditions and molecular weight, crucial for understanding trehalose metabolism.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • Trehalase (E.C.3.2.1.28) is an enzyme that hydrolyzes trehalose.
    • Understanding trehalase function is important for metabolic studies.

    Purpose of the Study:

    • To isolate and purify trehalase from mouse kidney.
    • To characterize the biochemical and physical properties of the purified enzyme.

    Main Methods:

    • Enzyme isolation and purification using n-octanol, ammonium sulfate precipitation, and chromatography (DEAE-cellulose, SP-Sephadex, Sephadex G-200).
    • Homogeneity confirmed by gel electrophoresis.
    • Molecular weight estimation via gel filtration.
    • Enzyme kinetics and stability assays.

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    Main Results:

    • A 1700-fold purification of homogeneous trehalase was achieved.
    • The enzyme is specific for trehalose.
    • Estimated molecular weight is 73,000 Da.
    • Km for trehalose is 2.67 x 10(-3)M.
    • Optimum pH is 5.5-5.6 and optimum temperature is 60°C.

    Conclusions:

    • Mouse kidney trehalase has been successfully purified and characterized.
    • The enzyme exhibits specific activity towards trehalose with defined kinetic and stability parameters.
    • These findings provide a basis for further investigation into trehalase's physiological role.