OPTIMIZATION OF SYNTHESIS OF AGAROSE-BASED LECTIN AFFINITY SORBENTS

Different amounts of wheat germ agglutinin were immobilized to agarose gel, previously activated by different amounts of the coupling agent divinyl sulfone. The effectiveness of these affinity sorbents was char acterized by specific binding of ovomucoid with the gel. These studies revealed the formation of clear optima in binding capacity of the aff inity gel, depending on conditions of its synthesis. The ratio between the concentration of the coupling agent and immobilized lectin were f ound to be crucial for optimization of binding properties of the affin ity sorbent.