Kallikrein-like enzyme from the venom of Agkistrodon p. piscivorus.
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.
Nikai
T
T
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
Imai
K
K
Nagasaka
M
M
Sugihara
H
H
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
D000596:Amino Acids; D012910:Snake Venoms; D005340:Fibrinogen; D007610:Kallikreins