A new lectin from tulip (Tulipa) bulbs.
A lectin was isolated from tulip (Tulipa) bulbs by affinity chromatography on fetuin-agarose and partially characterized. The tulip lectin is a tetrameric protein composed of four identical subunits of Mr 28 000, which are not held together by disulphide bonds. It is not glycosylated and has an amino-acid composition typified by a high content of asparagine-aspartic acid, leucine, glycine and serine. Tulip lectin agglutinates human red blood cells, but has a much higher specific activity with rabbit erythrocytes. In hapten-inhibition assays with the latter type of red blood cell the lectin exhibits a complex specificity, whereas its agglutination with human erythrocytes is readily inhibited by N-acetylgalactosamine, lactose, fucose and galactose.
Laboratorium voor Plantenbiochemie, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3030, Leuven, Belgium.
B P
BP
Cammue
B
B
Peeters
W J
WJ
Peumans