Díaz A, Henriques O B
Acta Physiol Lat Am. 1976;26(4):248-53.
Kininogens I (HMW) and II (LMW) were isolated and partially purified from human plasma. The disappearance of kininogen I was prevented by the use of hexadimethrine bromide, which inhibits the activation of plasma prekallikrein. The two kininogens were separated by chromatography on DEAE-cellulose. Further purification of kininogen I and II was achieved by separate chromatographic steps of the partially purified kininogens on SP-Sephadex. The purification of the kininogens was controlled by incubation of the respective samples with different kininogenases: human plasma kallikrein, human salivary kallikrein and trypsin. As determined by gel filtration, a molecular weight of 250 000 daltons was found for kininogen I (HMW) and 48 000 daltons for kininogen II (LMW).
从人血浆中分离并部分纯化了激肽原I（高分子量）和II（低分子量）。使用抑制血浆前激肽释放酶激活的溴化六甲双铵可阻止激肽原I的消失。通过在DEAE - 纤维素上进行色谱分离将两种激肽原分开。通过将部分纯化的激肽原在SP - 葡聚糖凝胶上进行单独的色谱步骤，进一步纯化了激肽原I和II。通过将各个样品与不同的激肽原酶（人血浆激肽释放酶、人唾液激肽释放酶和胰蛋白酶）一起孵育来控制激肽原的纯化。通过凝胶过滤测定，发现激肽原I（高分子量）的分子量为250000道尔顿，激肽原II（低分子量）的分子量为48000道尔顿。
