Biochemical Studies

Interaction of the Laburnum anagyroides Lectin with Fucoantigens

V. E. Piskarev^1#, T. L. Bushueva² and I. A. Yamskov¹

^#Phone/fax: (495) 135-93-75; e-mail: piskarev@ineos.ac.ru

¹Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, ul. Vavilova 28, Moscow, 117813, Russia;
²Institute of Experimental Cardiology, Russian Cardiological Center, Moscow, ul. Tret’ya Cherepkovskaya 15a, Moscow, 121552, Russia

Received: July 18, 2006; in final form: September 4, 2006

Abstract. We studied interaction of the lectin from the bark of Golden Rain shrub (Laburnum anagyroides, LABA) with a number of basic fucose-containing carbohydrate antigens by changes in its tryptophan fluorescence. The strongest LABA binding was observed for the trisaccharide H of type 6 [α-L-Fucp-(1-2)-β-D-Galp-(1-4)-D-Glc, K_a = 4.2 × 10³ M⁻¹]. The following antigens were bound with a weaker affinity: H-disaccharide α-L-Fucp-(1-2)-D-Gal, a glucoanalogue of tetrasaccharide Le^y α-L-Fucp-(1-2)-β-D-Galp-(1-4)-[α-L-Fucp-(1-3)]-D-Glc, and 6-fucosyl-N-acetylglucosamine, a fragment of core of the N-glycans family (K_a = (1.1−1.7) × 10³ M⁻¹). The lowest binding was observed for L-fucose (K_a = 2.7 × 10² M⁻¹) and trisaccharide Le^a, (β-Galp-(1-3)-[α-L-Fucp-(1-4)]-GlcNAc (K_a = 6.4 × 10² M⁻¹). The Le^d, Le^a, and Le^x pentasaccharides and Le^b hexasaccharide were not bound to LABA.

Key words: Laburnum anagyroides lectin, carbohydrate specificity, fucoantigens

Russian Journal of Bioorganic Chemistry 2007, 33 (1): 170-174