Chemical-modification studies of a unique sialic acid-binding lectin from the snail Achatina fulica. Involvement of tryptophan and histidine residues in biological activity.

@article{Basu1988ChemicalmodificationSO,
  title={Chemical-modification studies of a unique sialic acid-binding lectin from the snail Achatina fulica. Involvement of tryptophan and histidine residues in biological activity.},
  author={S. Basu and C. Mandal and A. Allen},
  journal={The Biochemical journal},
  year={1988},
  volume={254 1},
  pages={
          195-202
        }
}
  • S. Basu, C. Mandal, A. Allen
  • Published 1988
  • Chemistry, Medicine
  • The Biochemical journal
  • A unique sialic acid-binding lectin, achatininH (ATNH) was purified in single step from the haemolymph of the snail Achatina fulica by affinity chromatography on sheep submaxillary-gland mucin coupled to Sepharose 4B. The homogeneity was checked by alkaline gel electrophoresis, immunodiffusion and immunoelectrophoresis. Amino acid analysis showed that the lectin has a fairly high content of acidic amino acid residues (22% of the total). About 1.3% of the residues are half-cystine. The… CONTINUE READING
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    Sialic acid binding lectins
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    References

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