Isolation and characterization of hemorrhagic metalloproteinase from Vipera berus berus (common viper) venom.

Samel M, Siigur J

Institute of Chemical Physics and Biophysics, Estonian Academy of Sciences, Tallinn, U.S.S.R.

Comp Biochem Physiol C Comp Pharmacol Toxicol. 1990;97(2):209-14. doi: 10.1016/0742-8413(90)90129-w.

Abstract

Hemorrhagic metalloproteinase (HMP) was isolated by gel filtration on a Sephadex G-100 (superfine) and affinity chromatography on agarose HPS-7. 2. Hemorrhagic metalloproteinase is a glycoprotein with mol. wt 56.3 kDa. It contains 1 zinc atom per molecule of protein. 3. Hemorrhagic metalloproteinase hydrolyzes casein, fibrinogen and splits the insulin B chain at positions Ala14-Leu15, Tyr16-Leu17, His10-Leu11. It digests A alpha chain of fibrinogen.

摘要