Sialic acid specific lectins from Episesarma tetragonum (Decapoda, Grapsidae): isolation, purification and characterization
| Autor: | R. Viswambari Devi, M.R. Basil Rose, P.D. Mercy |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: | |
| Zdroj: | International Journal of Aquatic Biology, Vol 1, Iss 4, Pp 150-157 (2013) |
| Druh dokumentu: | article |
| ISSN: | 2383-0956 2322-5270 |
| Popis: | Two sialic acid specific lectins Episesarma tetragonum agglutinin–1 and 2 were purified from the hemolymph of the Mangrove crab, Episesarma tetragonum. 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. |
| Databáze: | Directory of Open Access Journals |
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