Díaz A, Henriques O B
Acta Physiol Lat Am. 1976;26(4):243-7.
Plasma supernatant in which kallikrein has been activated and removed by glass powder whilst kininogen I (HMW) has been consumed by the activated kallikrein, was used for the preparation of kininogen II. It was purified by chromatography on DEAE-cellulose followed by gel filtration on G-200 Sephadex. The purification of kininogen II was assessed from determinations of the amount of kinin released (expressed as bradykinin) as measured on the isolated guinea pig ileum, using samples incubated with human salivary kallikrein or trypsin. A preparation of kininogen II containing an activity equivalent to 8 microgram Br/mg protein, was obtained. Salivary kallikrein released approximately three times more kinin from the substrate as compared to trypsin.
血浆上清液用于制备激肽原II，其中激肽释放酶已被玻璃粉激活并去除，而激肽原I（高分子量）已被激活的激肽释放酶消耗。通过在DEAE-纤维素上进行色谱分离，然后在G-200葡聚糖凝胶上进行凝胶过滤对其进行纯化。使用与人唾液激肽释放酶或胰蛋白酶孵育的样品，通过测定在分离的豚鼠回肠上测量的激肽释放量（以缓激肽表示）来评估激肽原II的纯化情况。获得了一种激肽原II制剂，其活性相当于8微克缓激肽/毫克蛋白质。与胰蛋白酶相比，唾液激肽释放酶从底物释放的激肽大约多三倍。
