Biological properties of kinin-releasing enzyme from Trimeresurus okinavensis (himehabu) venom.
A kinin-releasing enzyme was isolated and characterized from the venom of Trimeresurus okinavensis (himehabu) using Sephadex G-100, DEAE-Cellulose, and CM-Cellulose column chromatographies. The kinin-releasing enzyme was homogeneous as demonstrated by a single band on polyacrylamide gel electrophoresis, and isoelectric focusing. The enzyme possesses a molecular weight of 31,000 Da and isoelectric point of 8.2 and consists of 312 total amino acid residues. Specific esterolytic activities of the kinin-releasing enzyme on N-tosyl-L-arginine methyl ester (TAME) and N-benzoyl-L-arginine ethylester (BAEE) were determined to be 235.3 and 111.3 mumol/min/mg, respectively. The enzyme was inhibited by p-APMSF (p-amidinophenylmethanesulfonyl fluoride hydrochloride) and benzamidine. Additionally, the enzyme was found stable to heat treatment. The enzyme cleaved a kininogen analog with the release of bradykinin, resulting in an immediate drop in blood pressure, and contractions of the rat uterus were also observed.
Nikai
T
T
Faculty of Pharmacy, Meijo University, Nagoya, Japan. nikai@meijo-u.ac.jp
Komori
Y
Y
Kato
S
S
Sugihara
H
H
D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry / Q000201:enzymology*; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry; D007704:Kininogens / Q000378:metabolism; D007705:Kinins / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000378:metabolism; D008970:Molecular Weight; D051381:Rats; D017841:Trimeresurus
D003435:Crotalid Venoms; D015853:Cysteine Proteinase Inhibitors; D007704:Kininogens; D007705:Kinins; D008666:Metalloendopeptidases