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.
Faculty of Pharmacy, Meijo University, Nagoya, Japan. nikai@meijo-u.ac.jp
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Nikai
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Komori
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Kato
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Sugihara
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