Isolation and characterization of a novel P-II class snake venom metalloproteinase from Trimeresurus stejnegeri.
Stejnitin, a novel class P-II snake venom metalloproteinase (SVMP) with a molecular weight of about 35kDa, was purified from Trimeresurus stejnegeri venom. The cDNA of stejnitin encoded a polypeptide of 295 amino acid residues which comprises a signal peptide, proprotein, metalloproteinase domain, spacer and disintegrin domain. The protein sequence deduced from cDNA was confirmed by peptide mass fingerprinting analysis. It is highly homologous to the members of subclass P-IIa SVMPs which comprises metalloproteinase and disintegrin together. Results from DNA fragmentation and flow cytometry analysis also indicated that stejnitin is able to induce apoptosis of ECV304 cells (R=0.908, P=0.012).
Han
Yao-Ping
YP
Department of Biology and Food Science, Changshu Institute of Technology, 98 Yuanhe Road, Changshu, Jiangsu 215500, China. hanyaop@yahoo.com.cn
Lu
Xiang-Yun
XY
Wang
Xue-Feng
XF
Xu
Juan
J
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis / Q000187:drug effects; D001483:Base Sequence; D003001:Cloning, Molecular; D003435:Crotalid Venoms / Q000201:enzymology*; D053938:DNA Fragmentation; D005434:Flow Cytometry; D006801:Humans; D045726:Metalloproteases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry / Q000302:isolation & purification; D016415:Sequence Alignment
D003435:Crotalid Venoms; D010975:Platelet Aggregation Inhibitors; C029748:Trimeresurus venoms; D045726:Metalloproteases