Isolation and characterization of hemorrhagic metalloproteinase from Vipera berus berus (common viper) venom.
1. 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.
Samel
M
M
Institute of Chemical Physics and Biophysics, Estonian Academy of Sciences, Tallinn, U.S.S.R.
Siigur
J
J
D000595:Amino Acid Sequence; D002364:Caseins / Q000378:metabolism; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005340:Fibrinogen / Q000378:metabolism; D007328:Insulin / Q000378:metabolism; D008666:Metalloendopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity; D014757:Viper Venoms / Q000032:analysis*; D015032:Zinc / Q000032:analysis
D002364:Caseins; D007328:Insulin; D014757:Viper Venoms; D005340:Fibrinogen; D008666:Metalloendopeptidases; C069317:hemorrhagic metalloproteinase; D015032:Zinc