AMINO-ACID-SEQUENCE OF A LECTIN-LIKE PROTEIN FROM LACHESIS-MUTA-STENOPHYRS VENOM

The primary structure of the lectin-like protein from Lachesis muta st enophyrs venom was deduced from analysis of the N-terminus and the seq uence of peptides obtained after digestion with trypsin, Arg-C enzyme, Staphylococcus aureus V8 protease and endoproteinase Asp-N. Peptides generated by cleavage of the lectin with cyanogen bromide and o-iodoso benzoic acid were also sequenced. Comparison of the complete 135 amino acid residues sequence with those of the lectin from the venom of Cro talus atrox, with platelet coagglutinin from Bothrops jararaca beta-fr agment and with the anticoagulant B protein chain from Trimeresurus fl avoviridis venom, revealed 92, 46 and 29% identity, respectively. Sign ificant homology was also found with C-type carbohydrate-recognition d omain-like structures from invertebrate and vertebrate lectins. To our knowledge, this is the second known primary structure of a lectin-lik e protein from snake venom. Copyright (C) 1996 Elsevier Science Ltd