A new lectin from tulip (Tulipa) bulbs

✍ Scribed by B. P. A. Cammue; B. Peeters; W.J. Peumans

• Book ID: 104752863
• Publisher: Springer-Verlag
• Year: 1986
• Tongue: English
• Weight: 635 KB
• Volume: 169
• Category: Article
• ISSN: 0032-0935
• DOI: 10.1007/bf00392110

✦ Synopsis

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.