Physicochemical characterization of hemagglutinin from the coelomic fluid of the Sea urchin Tripneustes gratilla (Linnaeus, 1758)

Author(s): *Rajaselvam J, Sr. M. R. Basil Rose and Jeni Chandar Padua

Abstract: Lectins are carbohydrate binding proteins with the ability to agglutinate cells. In this study, a naturally occurring hemagglutinin with specific affinity for dog erythrocytes was identified, isolated and purified from the coelomic fluid of the sea urchin Tripneustes gratilla. The physicochemical characteristics of the agglutinin showed that its hemagglutinating activity was calcium dependent, optimum at pH 7.5 and temperature between 0 to 30°C and in the presence of 1-10 mM CaCl2 or 5 mM MgCl2. The HA activity was reversibly sensitivity to di and tetra sodium EDTA. Cross adsorption assay of the agglutinin revealed the presence a single lectin. PSM was identified as the potent inhibitor followed by thyroglobulin, BSM, transferrin, and fetuin. The agglutinating activity of the agglutinin is also inhibited by the sugars α-lactose, D-fucose, sucrose, trechalose, L-fucose and melibiose.

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