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  • Title: Interaction of the alpha-mannosidase from Canavalia ensiformis with the lectin from the same plant, concanavalin A.
    Author: Einhoff W, Rüdiger H.
    Journal: Biol Chem Hoppe Seyler; 1986 Sep; 367(9):943-9. PubMed ID: 3790262.
    Abstract:
    The specific interaction between the lectin concanavalin A and the alpha-mannosidase from the Leguminosa Canavalia ensiformis was studied by means of laser nephelometry and affinity chromatography. Both proteins react optimally within a certain stoichiometrical range. Interaction is restricted to a narrow pH interval (around pH 5) and to low ionic strengths (less than 10mM NaCl). Neither the sugar-binding site of the lectin nor the catalytic and the hydrophobic sites of the enzyme participate in the interaction. The conformation of the enzyme at pH 5 which favours the interaction can be arrested by immobilization. After this, the enzyme is able to bind the lectin even at pH 8 where no interaction takes place between the dissolved proteins.
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