title: [Trypsin and chymotrypsin inhibitors from viper venom].
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.
authors.forename: E P
authors.initials: EP
authors.lastname: Siĭgur
authors.forename: M Iu
authors.initials: MIu
authors.lastname: Samel
authors.forename: Iu R
authors.initials: IuR
authors.lastname: Siĭgur
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D014361:Trypsin Inhibitors / Q000302:isolation & purification*; D014757:Viper Venoms / Q000032:analysis*; D000514:alpha 1-Antichymotrypsin / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D014361:Trypsin Inhibitors; D014757:Viper Venoms; D000514:alpha 1-Antichymotrypsin
vernacular_title: Ingibitory tripsina i khimotripsina iz iada gadiuki.