Abstract
—During the isolation of a capillary permeability-increasing enzyme from the venom of A. caliginosus, a kininogenase was also purified from the venom by gel filtration on Sephadex G-100, ion-exchange chromatographies on CM-Sephadex C-50 and DEAE-Sephadex A-50, and gel filtration on Sephadex G-75. By this procedure, 11 mg of the purified enzyme were obtained from 4 g of the venom. The purified enzyme was homogeneous by polyacrylamide disc gel electrophoresis at pH 8.3 and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and did not show any caseinolytic or clotting activity. The purified enzyme released bradykinin from purified bovine high mol.wt kininogen. The capillary permeability was increased by injection of the purified enzyme into the depilated skin of the back of a rabbit. It is supposed that the capillary permeability-increasing activity exerted by the enzyme is due to the release of bradykinin.
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