Sekoguchi S, Nikai T, Suzuki Y, Sugihara H
Biochim Biophys Acta. 1986 Dec 10;884(3):502-9. doi: 10.1016/0304-4165(86)90201-1.
A kinin-releasing enzyme was isolated from Bitis arietans (puff adder) venom by Sephadex G-100 and DEAE-cellulose column chromatographies. The kinin-releasing enzyme was shown to be homogeneous as demonstrated by a single band on acrylamide gel electrophoresis, isoelectric focusing, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunodiffusion. Its molecular mass is approximately 45 kDa with an isoelectric point of 6.5. Kinin-releasing enzyme possesses proteolytic activity which hydrolyzes the Leu6-Cys7, His10-Leu11 and Ala14-Leu15 bonds of the B chain of oxidized insulin and the A alpha and B beta chain of fibrinogen. Kinin-releasing and benzoyl-L-arginine ethyl ester hydrolytic activities of this enzyme were inhibited by diisopropyl fluorophosphate, suggesting that the serine hydroxyl group is involved in enzymatic activities.
通过葡聚糖凝胶G - 100和二乙氨基乙基纤维素柱色谱法从鼓腹咝蝰毒液中分离出一种激肽释放酶。经丙烯酰胺凝胶电泳、等电聚焦、十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳和免疫扩散显示，该激肽释放酶呈现均一性。其分子量约为45 kDa，等电点为6.5。激肽释放酶具有蛋白水解活性，可水解氧化胰岛素B链的Leu6 - Cys7、His10 - Leu11和Ala14 - Leu15键以及纤维蛋白原的Aα和Bβ链。该酶的激肽释放活性和苯甲酰 - L - 精氨酸乙酯水解活性受到二异丙基氟磷酸的抑制，这表明丝氨酸羟基参与了酶活性。
