Amino acid sequence of a lectin-like protein from Lachesis muta stenophyrs venom

被引:32
作者
AragonOrtiz, F [1 ]
Mentele, R [1 ]
Auerswald, EA [1 ]
机构
[1] UNIV MUNICH, CLIN CTR CITY, DEPT CLIN CHEM & CLIN BIOCHEM, D-8000 MUNICH 2, GERMANY
关键词
D O I
10.1016/0041-0101(96)00011-6
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
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. Copyright (C) 1996 Elsevier Science Ltd
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页码:763 / 769
页数:7
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