AFFINITY PURIFICATION OF N-ACETYLGLUCOSAMINE SPECIFIC LECTINS - PURIFICATION AND PARTIAL CHARACTERIZATION OF TRITICALE LECTIN

Seeds of Triticale contain a lectin that agglutinates rabbit erythrocy tes whose activity is inhibited by N-Acetylglucosamine and its oligome rs. An affinity method has been developed that efficiently binds the l ectin activities from Triticale seeds and wheatgerm. Purified Tritical e lectin isa glycoprotein with 3% carbohydrate and migrates as a singl e band corresponding to Mr. 15000 on SDS-PAGE. Antibodies raised to pu rified wheat germ agglutinin do not cross-react with purified Tritical e lectin. Leucine/Isoleucine is the only N-terminal residue in the Tri ticale lectin. Presence of inhibitory sugar induces spectral changes i n the protein in the UV region. Triticale lectin does not agglutinate human ABO erythrocytes and does not inhibit fungal growth.