Interaction of the alpha-mannosidase from Canavalia ensiformis with the lectin from the same plant, concanavalin A.
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.
D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism; D007887:Fabaceae / Q000378:metabolism; D007700:Kinetics; D008361:Mannosidases / Q000378:metabolism*; D009391:Nephelometry and Turbidimetry / Q000379:methods; D037121:Plant Lectins; D010944:Plants / Q000378:metabolism*; D010946:Plants, Medicinal; D011485:Protein Binding; D043323:alpha-Mannosidase
D004800:Enzymes, Immobilized; D037121:Plant Lectins; D003208:Concanavalin A; D008361:Mannosidases; D043323:alpha-Mannosidase