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Further biochemical and biophysical characterisation of scyllin, Scylla serrata hemolymph lectin
Author(s) -
Chattopadhyay Tinku,
Chatterjee Bishnupada
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700202571
Subject(s) - hemolymph , scylla serrata , lectin , biochemistry , tryptophan , glycoprotein , ceruloplasmin , chemistry , amino acid , mannose , biology , ecology
The amino acid and carbohydrate analysis of scyllin, a low molecular weight lectin purified from Scylla serrata (edible crab) haemolymph reveal that scyllin is rich in acidic and neutral amino acids and contains high amount of mannose. UV absorption of scyllin is perturbed by DMSO at 272 nm showing the presence of tryptophan molecule in scyllin exposed and accessible to the solvent. The oxidation of tryptophan molecule by N‐bromosuccinimide results in loss of haemagglutinating activity of lectin. The study of thermodynamic parameters of scylin‐glycoproteins interaction suggests that ceruloplasmin is the most potent inhibitors of scyllin of all the glycoproteins studied.