Isolation and characterization of a bioactive lectin from Zizyphus oenoplia

Author : Ashwin B. Butle and M. B. Patil

A lectin isolated from Zizyphus oenoplia leaves, agglutinating rabbit and human B group erythrocytes, was purified to homogeneity by affinity chromatography on Guar gum column. The purified lectin showed single band, both in non-denaturing PAGE and SDS-PAGE. The molecular weight determined by SDS-PAGE was found to be 23000 Da. Treatment of lectin with 10 mM EDTA diminished the haemagglutinating activity to 50% of the original level. Addition of divalent cations, Mg2+ and Mn2+ at 1mM totally restored hemagglutinating activity. The protein shows maximum activity over the pH range and was stable at higher temperature. It was identified to be a glycoprotein. The lectin has shown to promote proliferation of human lymphocytes after 72 h of culture under standard conditions. The purified lectin was also found to be pH and temperature stable.

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