Abstract：
:A thrombin-like enzyme, named BjussuSP-I, isolated from Bothrops jararacussu snake venom, is an acidic single-chain glycoprotein with M(r)=61,000, pI approximately 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 696bp 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.
journal_name
Biochimiejournal_title
Biochimieauthors
Sant'Ana CD,Bernardes CP,Izidoro LF,Mazzi MV,Soares SG,Fuly AL,Zingali RB,Magro AJ,Braz AS,Fontes MR,Stábeli RG,Sampaio SV,Soares AMdoi
10.1016/j.biochi.2007.10.005subject
Has Abstractpub_date
2008-03-01 00:00:00pages
500-7issue
3eissn
0300-9084issn
1638-6183pii
S0300-9084(07)00298-2journal_volume
90pub_type
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