Study Of Plasminogen Activerin Agkistrodon Halysussuriensis Venom

Plasminogen activator changes plasminogen to plasminogen by cutting down a certain peptide. Venom plasminogen activator has a good future ,since it's half life is long and it's bleeding side-effect is small.In this study, we reicece a Venom plasminogen activator from Agkistrodon halysussuriensis venom using DEAE-Sephadex A-50 papreg, Sephadex G-75 papreg, Lysine Sepharose ^TM 4B papreg. After the assays of SDS-PAGE and HPLC, only one ingredient was detected. It's relative molecular weight is 32KD by using SDS-PAGE gel electrophoresis and it's isoelectric point is 4.82 by using equipotential electrophoresis.The protein is made of a single peptide. Vitriol- phenol and PAS show it has not glycosylation in it's component. Atom absorbence spectrum show it has five mol zinc per mol protein.the plasminogen activator was a kind of serine protease containing zinc. It had unique plasminogen activator activity, without arginine esterase, Fibrinolysin and haemorrhagia toxic activities. The best enzyme catalysis temperature and pH were 60 ℃ and 8 respectively. Its activity was not inhibited by plasma protease inhibitory factors. The measures of its enzymology and physiological characteristics established the foundation of its further pharmacolog evaluation.The study indicated the feasibility of the isolation of plasminogen activator from Agkistrodon halysussuriensis venom. It is possible that the purified plasminogen activator protein could be a new type thrombolysis agent. The further study is being carried out.