title: Kallikrein-like enzyme from the venom of Agkistrodon p. piscivorus.
abstract: 1. A kallikrein-like enzyme was isolated from Agkistrodon p. piscivorus venom by Sephadex G-100, DEAE-Sephacel and S-Sepharose column chromatographies. 2. A kallikrein-like enzyme was shown to be homogeneous as demonstrated by a single band on acrylamide gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunodiffusion. 3. Its molecular weight is approx. 29,000 with an isoelectric point of 7.8. 4. A kallikrein-like enzyme is able to cleave a kininogen analog to release bradykinin, and the B beta chain of fibrinogen. These proteolytic and tosyl-L-arginine methyl ester hydrolytic activities were inhibited by diisopropyl fluorophosphate, suggesting that the serine hydroxyl group is involved in enzymatic activities.
authors.affiliation: Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nikai
authors.forename: K
authors.initials: K
authors.lastname: Imai
authors.forename: M
authors.initials: M
authors.lastname: Nagasaka
authors.forename: H
authors.initials: H
authors.lastname: Sugihara
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000032:analysis; D006868:Hydrolysis; D007526:Isoelectric Point; D007610:Kallikreins / Q000276:immunology / Q000302:isolation & purification*; D008970:Molecular Weight; D012910:Snake Venoms / Q000032:analysis*; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D012910:Snake Venoms; D005340:Fibrinogen; D007610:Kallikreins