@article{Devi_Rose_Mercy_2013, title={Sialic acid specific lectins from Episesarma tetragonum (Decapoda, Grapsidae): isolation, purification and characterization}, volume={1}, url={https://ij-aquaticbiology.com/index.php/ijab/article/view/66}, DOI={10.22034/ijab.v1i4.66}, abstractNote={Two sialic acid specific lectins <em>Episesarma tetragonum</em> agglutinin–1 and 2 were purified from the hemolymph of the Mangrove crab, <em>Episesarma tetragonum</em>. The major lectin was purified using CNBr-activated sepharose 4B conjugated to fetuin. N-acetyl glucosamine containing buffer was used for elution. The hemagglutination activity of purified lectin was inhibited by glycoproteins containing Siaα, 2-3Galβ, 1-4 GlcNAc linkages. On SDS-PAGE, the molecular weight of calcium dependent lectin was observed to be 70 kDa. Lectin had the maximum activity at a wide range of pH (6.5 – 9.5) and temperature (0 - 40 °C).  The physicochemical characteristics of the minor agglutinin showed that its hemagglutinating activity was calcium dependent, optimum at pH 8 – 9.5 and temperature 0 – 37 °C. The only potent inhibitor of minor lectin was bovine submaxillary mucin. An attempt was also made to purify minor lectin by affinity chromatography using bovine submaxillary mucin coupled to CNBr-activated sepharose 4B column. The lectin was eluted with elution buffer containing ethylene diamine tetra acetate. Strong inhibition of purified minor lectin by bovine submaxillary mucin and non-inhibitory action of de-O-acetylated bovine submaxillary mucin suggested that the lectin was O-acetyl sialic acid specific.}, number={4}, journal={International Journal of Aquatic Biology}, author={Devi, R. Viswambari and Rose, M.R. Basil and Mercy, P.D.}, year={2013}, month={Jul.}, pages={150–157} }