Vol. 2, Issue 4 (2017)
Partial purification and characterization of hemolymph lectin of marine crab Atergatis ocyroe by adsorption on formalinized erythrocytes
Author(s): Elayabharathi, J Vinoliya Josephine Mary, S Mary Mettilda Bai
Abstract: Hemolymph lectin of marine crab Atergatis ocyroe was purified by biospecific adsorption using formalinized buffalo erythrocytes. SDS-PAGE of the lectin yielded two subunits of molecular masses 50 kDa and 25 kDa. The isolated lectin is a non-blood group specific lectin since it agglutinated both human and animal erythrocytes. The lectin showed high affinity towards buffalo and rabbit erythrocytes suggesting its specificity to bind to the sialic acids that are expressed on the erythrocytes. The hemagglutinin was calcium dependent and sensitive to pH, temperature and calcium chelator – EDTA. Hemagglutination inhibition assay revealed bovine thyroglobulin as the potent inhibitor followed by fetuin, BSM and PSM. Sugars like GlcNAc, Trehalose, D - Fructose, melibiose, L - Fucose and α – Lactose weakly inhibited the agglutinin. Based on the erythrocyte and glycoprotein specificity it could be concluded that the lectin is sialic acid specific which could be further purified using affinity chromatography and used in lectin targeted therapy.