Title of article :
The specificity of the binding site of AchatininH, a sialic acid-binding lectin from Achatina fulica
Author/Authors :
Goutam Sen، نويسنده , , Chitra Mandal، نويسنده ,
Issue Information :
دوهفته نامه با شماره پیاپی سال 1995
Pages :
11
From page :
115
To page :
125
Abstract :
A sialic acid-binding lectin, AchatininH (ATNH), having unique specificity towards 9-O-acetylneuraminic acid, has been purified and characterized. The specificity of this lectin for O-acetylsialic acids was studied in detail, using various sialic acid derivatives and sialoglycoproteins. The potent inhibition of hemagglutination by bovine submaxillary mucin (BSM), which contains 9(7,8)-O-acetylsialic acid and by free 9-O-acetylneuraminic acid confirms the preferential affinity towards this sugar. Further support for the role of O-acetylsialic acid was obtained by sialidase treatment of BSM. O-Deacetylation of the sialic acid residue abolished its inhibitory potency. Moreover, when the trihydroxypropyl side chain of the sialic acid molecule was modified by periodate-borohydride treatment, the truncated C7-sialic acid was unable to bind ATNH. This result suggests that the glycerol side chain of Neu5Ac, especially the C-8 and/or C-9 portion is an important determinant for ATNH. The hemagglutination-inhibition results using several mono-, di-, and tri-saccharides containing terminal sialic acid and various sialoglycoproteins reveals that ATNH preferentially binds the α-(2 → 6)-linked sialic acid. Furthermore, β-D-GlcNAc-(1 → 3)-[α-NeuGc-(2 → 6)]-GalNAc-ol was found to be the best ligand for ATNH.
Keywords :
Achatina fulica , Lectin , sialic acid-binding
Journal title :
Carbohydrate Research
Serial Year :
1995
Journal title :
Carbohydrate Research
Record number :
960936
Link To Document :
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