Sampaio C A, Vidmar S, Hamaguchi A, Sampaio M U
Adv Exp Med Biol. 1986;198 Pt B:105-11. doi: 10.1007/978-1-4757-0154-8_13.
Active plasma kallikrein (Mr = 90,000) can be separated by reduction of the disulfide bridges into a heavy-chain (Mr = 45,000) and a light-chain (Mr = 36,000). A partially active fragment, corresponding to the light-chain, was isolated during the purification of active human plasma kallikrein. Bovine trypsin can form a fragment corresponding to the heavy-chain when incubated with plasma kallikrein; plasmin also causes the formation of the heavy-chain but at a slower rate. High molecular weight kininogen decreases the rate of cleavage of kallikrein by both enzymes. Light-chain does not accumulate during incubation with these proteases and the heavy-chain, after prolonged incubation is also digested. Incubation of labelled active kallikrein with plasma causes formation of fragments corresponding to the heavy- and the light-chain.
活性血浆激肽释放酶（分子量=90,000）可通过还原二硫键分离为重链（分子量=45,000）和轻链（分子量=36,000）。在活性人血浆激肽释放酶的纯化过程中，分离出了一个与轻链相对应的部分活性片段。牛胰蛋白酶与血浆激肽释放酶一起孵育时可形成一个与重链相对应的片段；纤溶酶也会导致重链的形成，但速度较慢。高分子量激肽原会降低这两种酶对激肽释放酶的切割速率。与这些蛋白酶孵育时轻链不会积累，长时间孵育后重链也会被消化。用血浆孵育标记的活性激肽释放酶会导致形成与重链和轻链相对应的片段。
