1. [Trypsin and chymotrypsin inhibitors from viper venom].
- Author
-
Siĭgur EP, Samel MIu, and Siĭgur IuR
- Subjects
- Amino Acids analysis, Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Kinetics, Trypsin Inhibitors isolation & purification, Viper Venoms analysis, alpha 1-Antichymotrypsin isolation & purification
- Abstract
Inhibitors of trypsin and alpha-chymotrypsin with Mr of about 7000 Da and isoelectric points of greater than 10 and 9.9, respectively, were isolated from the venom of the common viper Vipera berus berus, using gel filtration and ion exchange chromatography. The inhibitor I prefers alpha-chymotrypsin (Ki = 4.6 X 10(-10) M) for the formation of an enzymeinhibitor complex at a molar ratio of 1:1. The inhibitor II prefers trypsin (Ki = 6.7 X 10(-11) M), forms an EI-complex at a molar ratio of 1:2, but also inhibits alpha-chymotrypsin (Ki = 1.4 X 10(-9) M) and hog pancreatic kallikrein (Ki = 1.6 X 10(-8) M). The inhibitor II contains no valine or methionine.
- Published
- 1988