STUDIES ON SNAKE VENOMS .17. PROPERTIES OF BRADYKININ RELEASING ENZYME IN VENOM OF AGKISTRODON HALYS BLOMHOFFII
STUDIES ON SNAKE VENOMS .17. PROPERTIES OF BRADYKININ RELEASING ENZYME IN VENOM OF AGKISTRODON HALYS BLOMHOFFII
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DOI：
10.1093/oxfordjournals.jbchem.a128173
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发表时间：
1965-01-01
影响因子：
2.7
通讯作者：
SUZUKI, T
中科院分区：
文献类型：
--
作者：
IWANAGA, S;SATO, T;SUZUKI, T
通过氟磷酸二异丙基（DFP）抑制、热失活和[α]- n -苯甲酰- l-精氨酸2乙酯（BAEE）抑制缓激肽酶活性的实验，得出缓激肽原释放的缓激肽依赖于缓激肽释放酶（BR）的精氨酸酯（AE）水解活性。Trasylol是一种商业缓激肽抑制剂，抑制缓激肽原通过蛇毒br酶释放缓激肽。而trasylol对毒液凝血酶和毛细血管通透性增加酶的AE水解活性没有影响。部分纯化的br -酶不需要金属离子。酶活性最适pH为8.5，在中性溶液中最稳定。br -酶的这些性质与胰激肽素的性质相似[EC 3.4.21]。
From experiments on diisopropyl fluoro-phosphate (DFP)-inhibition, heat-inactivation and [alpha]-N-benzoyl-L-arginine 2 ethylester (BAEE)-inhibition of enzyme activity, it was concluded that the release of bradykinin from bradykininogen is dependent upon the arginine ester (AE)-hydrolytic activity of the bradykinin releasing-(BR)-enzyme. Trasylol, a commercial kallikrein inhibitor, inhibited the release of bradykinin from bradykininogen by the venom BR-enzyme. However, trasylol had no effect on the AE hydrolytic activities of the clotting and capillary permeability increasing enzyme of the venom. The partially purified BR-enzyme did not require metal ions. The pH optimum for activity was 8.5 and the enzyme was most stable in neutral solution. These properties of the BR-enzyme are similar to those of pancreatic kallikrein [EC 3.4.4.21].