Some properties of a capillary permeability-increasing enzyme-2 from the venom of Agkistrodon caliginosus (Kankoku-Mamushi).
Capillary permeability-increasing enzyme-2 (CPI-enzyme-2) consists of a single polypeptide chain with an isoelectric point of pH 3.5. The enzyme is composed of 369 amino acid residues, based on a mol. wt of 44,000, and contains 20.3% carbohydrate. Both arginine ester hydrolytic and capillary permeability-increasing activities of the enzyme were inhibited by treatment with diisopropylfluorophosphate, indicating that the enzyme is a serine proteinase. The N-terminal amino acid sequence shows homology with that of CPI-enzyme-1 and similarity to those of batroxobin or kallikrein-like enzyme from other snake venoms.
Shimokawa
K
K
Division of Chemistry of Hygiene, Meiji College of Pharmacy, Tokyo, Japan.
Takahashi
H
H
D017836:Agkistrodon; D000581:Amidohydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002199:Capillary Permeability / Q000187:drug effects*; D002240:Carbohydrate Sequence; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D003435:Crotalid Venoms / Q000201:enzymology*; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity
D003435:Crotalid Venoms; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases; D012697:Serine Endopeptidases; C085657:capillary permeability-increasing enzyme 2; D000581:Amidohydrolases; C019665:amidase