Some properties of a proteolytic enzyme from the venom of Agkistrodon caliginosus (kankoku-mamushi) which increases capillary permeability

Abstract

Y. Ohtani and H. Takahashi. Some properties of a proteolytic enzyme from the venom of Agkistrodon caliginosus (kankoku-mamushi) which increases capillary permeability. Toxicon 26, 181 – 190, 1998. — The molecular weight of the capillary permeability-increasing enzyme from the venom of A. caliginosus was estimated to be about 32,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This enzyme consists of a single polypeptide chain with an isoelectric point of pH 4.80. The enzyme is composed of 266 amino acid residues, based on a molecular weight of 32,000, and contained 11.4% carbohydrate. The enzyme more readily hydrolyzed arginine esters than lysine esters and did not hydrolyze tyrosine ester. Both the arginine ester hydrolytic and capillary permeability-increasing activities were inhibited by treatment with diisopropylfluorophosphate, indicating that the enzyme is an arginine esterase of the serine proteinase type. The substrate specificity of the enzyme toward synthetic chromogenic or fluorogenic substrates for mammalian serine proteinases and the pH and heat stabilities of the enzyme were also investigated.