Muller-Esterl W, Dittmann B, Fritz H, Lottspeich F, Henschen A
Adv Exp Med Biol. 1983;156:157-64.
Kininogens have been purified from human plasma to apparent homogeneity. Native human LMW kininogen is a single-chain (glyco-) protein of molecular weight 68,000, which is converted to a two-chain protein by limited proteolysis with tissue kallikrein to form a heavy chain (Mr 62,000) and a light chain (Mr 4,000). Human HMW kininogen represents a single chain (glyco-)protein of Mr 114,000 which is split into two chains of similar size (H-chain of Mr 58,000 and L-chain of Mr 62,000) by limited proteolysis with tissue kallikrein. Sequence analysis of the isolated L-chain of human MW kininogen indicates a partial homology to the corresponding fragment-1.2 of bovine HMW kininogen. Purified kininogens readily form self-aggregates ranging from dimer to hexamer (HMW kininogen) and from dimer to decamer (LMW kininogen), respectively. Self-association is completely reversible in the presence of dissociating agents. Preliminary evidence suggests that oligomerisation is mediated by the H-chain common to the two types of kininogens.
激肽原已从人血浆中纯化至表观均一。天然人低分子量激肽原是一种分子量为68,000的单链（糖）蛋白，通过组织激肽释放酶的有限蛋白水解作用转化为双链蛋白，形成重链（Mr 62,000）和轻链（Mr 4,000）。人高分子量激肽原是一种Mr 114,000的单链（糖）蛋白，通过组织激肽释放酶的有限蛋白水解作用被裂解为两条大小相似的链（Mr 58,000的重链和Mr 62,000的轻链）。对分离出的人低分子量激肽原轻链的序列分析表明，它与牛高分子量激肽原的相应片段-1.2有部分同源性。纯化的激肽原很容易形成从二聚体到六聚体（高分子量激肽原）和从二聚体到十聚体（低分子量激肽原）的自聚集体。在解离剂存在下，自缔合是完全可逆的。初步证据表明，寡聚化是由两种激肽原共有的重链介导的。
