Einhoff W, Rüdiger H
Biol Chem Hoppe Seyler. 1986 Sep;367(9):943-9. doi: 10.1515/bchm3.1986.367.2.943.
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.
通过激光散射比浊法和亲和色谱法研究了植物凝集素伴刀豆球蛋白A与豆科植物刀豆中的α-甘露糖苷酶之间的特异性相互作用。两种蛋白质在一定的化学计量范围内反应最佳。相互作用局限于狭窄的pH区间（约pH 5）和低离子强度（小于10mM NaCl）。凝集素的糖结合位点以及酶的催化位点和疏水位点均不参与相互作用。有利于相互作用的pH 5条件下酶的构象可通过固定化来稳定。在此之后，即使在溶解的蛋白质之间不发生相互作用的pH 8条件下，该酶仍能够结合凝集素。
