TAILIEUCHUNG - Báo cáo khoa học: Purification and characterization of a sialic acid specific lectin from the hemolymph of the freshwater crab Paratelphusa jacquemontii

A naturally occurring hemagglutinin was detected in the serum of the freshwater crab, Paratelphusa jacquemontii (Rathbun). Hemagglutination activity with different mam-malian erythrocytes suggested a strong affinity of the serum agglutinin for horse and rabbit erythrocytes. The most potent inhibitor of hemagglutination proved to be bovine submaxillary mucin. The lectin was purified by affinity chromatography using bovine submaxillary mucin-coupled agarose. The molecular mass of the purified lectin was 34 kDa as determined by SDS/PAGE | Eur. J. Biochem. 270 4348-4355 2003 FEBS 2003 doi Purification and characterization of a sialic acid specific lectin from the hemolymph of the freshwater crab Paratelphusa jacquemontii Maghil Denis P. D. Mercy Palatty N. Renuka Bai and S. Jeya Suriya Department of Zoology Holy Cross College Rochnagar Nagercoil Tamil Nadu India A naturally occurring hemagglutinin was detected in the serum of the freshwater crab Paratelphusa jacquemontii Rathbun . Hemagglutination activity with different mammalian erythrocytes suggested a strong affinity of the serum agglutinin for horse and rabbit erythrocytes. The most potent inhibitor of hemagglutination proved to be bovine submaxillary mucin. The lectin was purified by affinity chromatography using bovine submaxillary mucin-coupled agarose. The molecular mass of the purified lectin was 34 kDa as determined by SDS PAGE. The hemagglutination of purified lectin was inhibited by N-acetylneuraminic acid but not by N-glycolylneuraminic acid even at a concentration of 100 mM. Bovine submaxillary mucin which contains mainly 9-ơ-acetyl- and 8 9 di-O-acety-N-acetyl neuraminic acid was the most potent inhibitor of the lectin. Sialidase treatment and de-O-acetylation of bovine submaxillary mucin abolished its inhibitory capacity completely. Also asialo-rabbit erythrocytes lost there binding specificity towards the lectin. The findings indicated an O-acetyl neuraminic acid specificity of the lectin. Keywords Paratelphusa jacquemontii hemolymph lectin sialic acid O-acetylsialic acid. Lectins are sugar-specific proteins with multiple combining sites capable of agglutinating cells or precipitating glycoconjugates 1 . Lectins may recognize specifically the whole sugar 2 a specific site in a sugar 3 a sequence of sugars 4 or their glycosidic linkages 5 on cell-surface glycoconjugates namely glycoproteins and glycolipids or in bacterial polysaccharides. Sialic acids are a family of sugars N-acetylneuraminic acid .

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