Affinity purification of N-acetylglucosamine specific lectins. Purification and partial charactersation of triticale lectin.
Seeds of Triticale contain a lectin that agglutinates rabbit erythrocytes whose activity is inhibited by N-Acetylglucosamine and its oligomers. An affinity method has been developed that efficiently binds the lectin activities from Triticale seeds and wheatgerm. Purified Triticale lectin is a glycoprotein with 3% carbohydrate and migrates as a single band corresponding to Mr. 15000 on SDS-PAGE. Antibodies raised to purified wheat germ agglutinin do not cross-react with purified Triticale lectin. Leucine/Isoleucine is the only terminal residue in the Triticale lectin. Presence of inhibitory sugar induces spectral changes in the protein in the UV region. Triticale lectin does not agglutinate human ABO erythrocytes and does not inhibit fungal growth.
Nadimpalli
S K
SK
Protein Biochemistry Laboratory, Department of Biochemistry, School of Life Sciences, University of Hyderabad, India.
Kompella
P
P
D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D002846:Chromatography, Affinity; D006801:Humans; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism; D037121:Plant Lectins; D010944:Plants; D011817:Rabbits
D037102:Lectins; D037121:Plant Lectins; D000117:Acetylglucosamine