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Related Experiment Videos

alpha-D-mannosidase forms in chicken liver.

L Lucas, J Martin-Barrientos, J A Cabezas

    The International Journal of Biochemistry
    |January 1, 1984
    PubMed
    Summary

    Two forms of alpha-D-mannosidase were isolated from embryonic chicken liver, with a third form appearing later. These enzymes exhibit distinct pH optima, heat stability, and responses to metal ions and inhibitors.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Alpha-D-mannosidase is a key enzyme involved in glycoprotein metabolism.
    • Understanding different forms of this enzyme is crucial for elucidating its biological roles.

    Purpose of the Study:

    • To isolate and characterize different forms of alpha-D-mannosidase from embryonic chicken liver.
    • To investigate the biochemical properties including pH optima, heat stability, and cofactor/inhibitor effects.

    Main Methods:

    • Ion-exchange chromatography on DEAE-cellulose was used for enzyme separation.
    • Enzyme activity assays were performed under varying pH conditions.
    • Heat stability and inhibition studies were conducted using specific ions and substrates.

    Main Results:

    • Three forms (I, II, and III) of alpha-D-mannosidase were identified, with form III absent in embryos.
    • Form I had an optimum pH of 5.0, form II (neutral) at 6.5, and form III at 4.5.
    • Forms I and III were heat-stable, while form II was unstable. Zn2+ and Mg2+ activated forms I and II, Co2+ affected them differently, and various compounds inhibited enzyme activity.

    Conclusions:

    • Embryonic chicken liver possesses distinct alpha-D-mannosidase forms with unique biochemical characteristics.
    • These findings provide insights into the developmental regulation and enzymatic properties of alpha-D-mannosidase.

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