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alpha-Mannosidase from Phaseolus vulgaris. Composition and structural properties

E Paus

    European Journal of Biochemistry
    |February 15, 1977
    PubMed
    Summary

    Phaseolus vulgaris alpha-mannosidases I and II are glycoproteins containing zinc. Alpha-mannosidase II exhibits greater thermal stability and carbohydrate content than alpha-mannosidase I.

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    Area of Science:

    • Biochemistry
    • Plant Science
    • Enzymology

    Background:

    • Alpha-mannosidases are crucial enzymes involved in glycoprotein metabolism.
    • Understanding the structural and biochemical properties of plant-derived alpha-mannosidases is important for their potential applications.

    Purpose of the Study:

    • To characterize and compare alpha-mannosidases I and II from Phaseolus vulgaris.
    • To investigate the structural features and biochemical properties of these enzymes.

    Main Methods:

    • Equilibrium sedimentation analysis in guanidine hydrochloride.
    • Electrophoresis in dodecyl sulfate and alkaline electrophoresis.
    • Electron microscopy.

    Main Results:

    • Both enzymes have molecular weights of 210-220 kDa and contain ~2 mol zinc/mol protein.
    • Alpha-mannosidase II has higher serine content and 16.5% carbohydrate, showing greater thermal stability than alpha-mannosidase I (8.3% carbohydrate).
    • The enzymes are composed of two ~110 kDa subunits, visualized as parallel rod-shaped monomers (7.4 nm x 4.2 nm x 4.2 nm) by electron microscopy.

    Conclusions:

    • Phaseolus vulgaris alpha-mannosidases I and II are distinct glycoproteins with different structural and stability characteristics.
    • The dimeric structure of these enzymes has been elucidated.

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