Isolation and physiological action of capillary permeability increasing-enzyme from the venom of Agkistrodon caliginosus.
A purified capillary permeability increasing-enzyme was obtained from Agkistrodon caliginosus venom by modification of our previous purification method. The purified enzyme, which had arginine esterase activity and strong capillary permeability increasing-activity, did not show caseinolytic, clotting or bradykinin-releasing activities. These properties of the enzyme were almost the same as those of the enzyme obtained by the previous purification method. When a mixture of the purified enzyme and bovine plasma or heated bovine plasma was injected into depilated skin on the back of a rabbit, the capillary permeability increasing-activity was much greater than that induced by injection of the enzyme alone. The substance which increases the capillary permeability was extracted from the incubated mixture of bovine plasma and the enzyme with 50-70% ethanol. Its activity was lost on treatment with carboxypeptidase A. From these results, it is supposed that the increase in capillary permeability induced by the enzyme is due to a low molecular weight peptide released from a protein in bovine plasma by the proteolytic action of the enzyme.
D000818:Animals; D002199:Capillary Permeability / Q000187:drug effects*; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification / Q000494:pharmacology*; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003435:Crotalid Venoms / Q000302:isolation & purification / Q000494:pharmacology*; D011817:Rabbits
C031442:Agkistrodon venoms; D003435:Crotalid Venoms; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases