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Zoological Research
Kunming Institute of Zoology, Chinese Academy of Sciences
ISSN: 2095-8137
Vol. 26, No. 6, 2005, pp. 616-621
Bioline Code: zr05060
Full paper language: Chinese
Document type: Research Article
Document available free of charge

Zoological Research, Vol. 26, No. 6, 2005, pp. 616-621

 en Purification and Characterization of Jerdonitin, a Non-hemorrhagic Metalloproteinase from Trimeresurus jerdonii check for this species in other resources Venom
CHEN Run-qiang, JIN Yang, WU Jian-bo, ZHONG Shu-rong, ZHU Shao-wen, LU Qiu-min1 et al.


Previously, we have purified Jerdonitin from Trimeresurus jerdonii check for this species in other resources venom. Compared with other P-II class snake venom metalloproteinases (SVMPs), Jerdonitin has a primary structure comprising metalloproteinase and disintegrin domains. However, no hemorrhagic and fibrinogenolytic activities were detected for Jerdonitin. We thought that organic buffer of high performance liquid charamatography (HPLC) might affect its enzymatic activity. In this study, we purified Jerdonitin by another procedure excluding the HPLC. It was homogenous as judged by SDS-PAGE and had an apparent molecular weight of 36 kDa under non-reducing conditions and 38 kDa under reducing conditions, respectively. Like other typical metalloproteinases, Jerdonitin preferentially degraded alpha-chain of human fibrinogen and this fibrinogenolytic activity was completely inhibited by EDTA, but not by PMSF. It was interesting that Jerdonitin did not induce hemorrhage after intradermal injection in mice.

Trimeresurus jerdonii, SVMP, Hemorrhage, Fibrinogenolytic activity

© Copyright 2005 Kunming Institute of Zoology, the Chinese Academy of Sciences
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