title: Amino acid sequence of a lectin-like protein from Lachesis muta stenophyrs venom.
abstract: The primary structure of the lectin-like protein from Lachesis muta stenophyrs venom was deduced from analysis of the N-terminus and the sequence 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-iodosobenzoic acid were also sequenced. Comparison of the complete 135 amino acid residues sequence with those of the lectin from the venom of Crotalus atrox, with platelet coagglutinin from Bothrops jararaca beta-fragment and with the anticoagulant B protein chain from Trimeresurus flavoviridis venom, revealed 92, 46 and 29% identity, respectively. Significant homology was also found with C-type carbohydrate-recognition domain-like structures from invertebrate and vertebrate lectins. To our knowledge, this is the second known primary structure of a lectin-like protein from snake venom.
authors.affiliation: Department of Biochemistry, School of Medicine, University of Costa Rica, San José, Costa Rica.
authors.forename: F
authors.initials: F
authors.lastname: Aragón-Ortiz
authors.forename: R
authors.initials: R
authors.lastname: Mentele
authors.forename: E A
authors.initials: EA
authors.lastname: Auerswald
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017837:Bothrops; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000737:chemistry* / Q000235:genetics; D037102:Lectins / Q000737:chemistry; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000378:metabolism; D013211:Staphylococcus aureus / Q000201:enzymology; D014357:Trypsin / Q000378:metabolism; D017819:Viperidae
chemical_list: D003435:Crotalid Venoms; D037102:Lectins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin