Previously, we have purified Jerdonitin from Trimeresurus jerdonii
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.