Purification of a kininogenase (kininogenase-2) from the venom of Agkistrodon caliginosus (Kankoku-Mamushi).
From the partially purified capillary permeability-increasing enzyme obtained from A. caliginosus venom, another kininogenase (kininogenase-2) was purified by gel filtration on Sephadex G-100 and ion-exchange chromatography on CM-Sephadex C-50, DEAE-Sephadex A-50, S-Sepharose Fast Flow and Q-Sepharose Fast Flow. The purified enzyme was homogeneous by polyacrylamide gel electrophoresis at pH 8.3 and SDS-gel electrophoresis. The kininogenase-2 had arginine ester hydrolytic and capillary permeability-increasing activities, and did not show any caseinolytic or clotting activity in a similar manner to a previously purified kininogenase (kininogenase-1). The purified kininogenase-2 liberated bradykinin on incubation with purified bovine high mol. wt kininogen. The rate of bradykinin release from the kininogen by kininogenase-2 was slower than that by the kininogenase-1, although both enzymes rapidly cleaved the peptide bonds in the kininogen molecule.
Yabuki
Y
Y
Meiji College of Pharmacy, Tokyo, Japan.
Oguchi
Y
Y
Takahashi
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001920:Bradykinin / Q000737:chemistry / Q000378:metabolism; D002199:Capillary Permeability / Q000187:drug effects; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003435:Crotalid Venoms / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D007610:Kallikreins / Q000302:isolation & purification* / Q000494:pharmacology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D012911:Snakes
D003435:Crotalid Venoms; D010446:Peptide Fragments; D007610:Kallikreins; D001920:Bradykinin