Activation of Sepharose with Epichiorohydrin and Subsequent Immobilization of Ligand for Affinity Adsorbent

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Abstract
The optimal conditions for the activation of Sepharose by epichiorohydrin and subsequent immobilization of ligands were investigated. Under the optimal conditions for activation, namely, 30% Sepharose-5 % epichlorohydrin-0·4 M NaOH, 40°C, 2 h, the maximum amount of epoxy group was introduced into Sepharose with low cross-linking. The adsorbents obtained by using N-acetyl-D-glucosamine, tri-N-acetylchitotriose, and glycoprotein as a ligand exhibited no nonspecific adsorption and good permeability for the high molecular substance to be purified, and were stable in an alkaline solution. Solanum tuberosum agglutinin was specifically adsorbed on a tri-N-acetylchitotriose-Sepharose column and was quantitatively recovered by elution with 0·2 M ammonia solution. Furthermore, the column could be repeatedly used under these conditions without reduction of its capacity.

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