Purification and properties of a proteinase from Vipera lebetina (snake) venom.
A proteinase from the venom of Vipera lebetina was purified by chromatography on Sephadex G-100 and CM-cellulose. The purified proteinase was homogeneous on SDS-polyacrylamide gel electrophoresis and consisted of a single chain with molecular weight of 37,000 +/- 1500. The isoelectric point of the proteinase was over 10. The enzyme was active on casein but not on esters and amides of arginine. It split the oxidized insulin B-chain at the peptide bonds of Tyr16-Leu17, Phe24-Phe25 and Phe25-Tyr26, and glucagon at the bonds Tyr10-Ser11, Leu14-Asp15 and Leu26-Met27. The enzyme was inhibited by DFP and PMSF, and partially by soybean trypsin inhibitor, but not with EDTA.
Mähar
A
A
Siigur
E
E
Siigur
J
J
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002845:Chromatography / Q000379:methods; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D005934:Glucagon / Q000378:metabolism; D006868:Hydrolysis; D007328:Insulin / Q000378:metabolism; D007526:Isoelectric Point; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis; D014757:Viper Venoms / Q000032:analysis*
D000596:Amino Acids; D007328:Insulin; D010446:Peptide Fragments; D014757:Viper Venoms; D005934:Glucagon; D010450:Endopeptidases