Abstract
Concanavalin A immobilized on chlorotriazine bead cellulose was applied to affinity purification of glycoenzymes and glycoproteins. Enzymes such as invertase from baker's yeast, endopolygalacturonase (Rohament P) and exopolygalacturonase from carrot roots, as well as extracellular mannoproteins from the yeast Cryptococcus laurentii were examined. Chromatography was performed on minicolumns filled with Concanavalin A-triazine bead cellulose gel with the content of immobilized Concanavalin A within the range 1.2 – 8.2 mg per mL of gel. The specifically bound glycoenzymes or glycoproteins were eluted with a solution of the corresponding counter-ligand a-methyl mannopyranoside. Individual degrees of purification, estimated from the measurements of specific activity of crude and purified glycoenzymes, were 14.5-fold for invertase, 93-fold for polygalacturonase and 3.9-fold for exopolygalacturonase. The yeast mannoprotein was isolated from the heteroglycoprotein fraction. The purified mannoprotein contained mainly mannose, with traces of glucose. The purification effect was verified by FPL-chromatography.
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