Biological properties of kinin-releasing enzyme from Trimeresurus okinavensis (himehabu) venom.

Journal of natural toxins Pub Date : 1998-02-01
T Nikai, Y Komori, S Kato, H Sugihara
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Abstract

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.

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姬哈布毒激肽释放酶的生物学特性。
利用Sephadex G-100、DEAE-Cellulose和CM-Cellulose色谱柱层析,从金斑蝶(Trimeresurus okinavensis, himahabu)毒液中分离得到一种激肽释放酶,并对其进行了结构表征。聚丙烯酰胺凝胶电泳和等电聚焦表明,激肽释放酶具有均匀性。该酶分子量为31,000 Da,等电点为8.2,由312个氨基酸残基组成。对n-甲酰基- l-精氨酸甲酯(TAME)和n-苯甲酰- l-精氨酸乙酯(BAEE),激肽释放酶的特异性酯分解活性分别为235.3和111.3 μ mol/min/mg。p-APMSF(对氨基苯基甲基磺酰氟盐酸盐)和苯并脒对该酶有抑制作用。此外,该酶对热处理也很稳定。该酶裂解激肽原类似物,释放缓激肽,导致血压立即下降,并观察到大鼠子宫收缩。
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