Molecular characterization of BjussuSP-I, a new thrombin-like enzyme with procoagulant and kallikrein-like activity isolated from Bothrops jararacussu snake venom

详细信息    查看全文

• 作者：Carolina D. Sant'Ana ; Carolina P. Bernardes ; Luiz Fern ; o M. Izidoro ; Maurí ; cio V. Mazzi ; S ; ro G. Soares ; André ; L. Fuly ; Russolina B. Zingali ; Angelo J. Magro ; Antonio S.K. Braz ; Marcos R.M. F
• 关键词：Thrombin-like enzyme ; Bothrops jararacussu ; Snake venom ; Proteolytic activity ; cDNA ; Glycosylation ; Structural characterization
• 刊名：Biochimie
• 出版年：2008
• 出版时间：March 2008
• 年：2008
• 卷：90
• 期：3
• 页码：500-507
• 全文大小：1225 K

文摘

A thrombin-like enzyme, named BjussuSP-I, isolated from Bothrops jararacussu snake venom, is an acidic single-chain glycoprotein with Mb>rb> = 61,000, pI border=0> 3.8 and 6 % sugar. BjussuSP-I shows high proteolytic activity upon synthetic substrates, such as S-2238 and S-2288. It also shows procoagulant and kallikrein-like activity, but is unable to act on platelets and plasmin. These activities are inhibited by specific inhibitors of this class of enzymes. The complete cDNA sequence of BjussuSP-I with 696 bp encodes open reading frames of 232 amino acid residues, which conserve the common domains of thrombin-like serine proteases. BjussuSP-I shows a high structural homology with other thrombin-like enzymes from snake venoms where common amino acid residues are identified as those corresponding to the catalytic site and subsites S1, S2 and S3 already reported. In this study, we also demonstrated the importance of N-linked glycans to improve thrombin-like activity of BjussuSP-I toxin.