人高分子量激肽原的特性。与无激肽高分子量激肽原轻链相关的促凝血活性。
Characterization of human high molecular weight kininogen. Procoagulant activity associated with the light chain of kinin-free high molecular weight kininogen.
作者信息
Thompson R E, Mandle R, Kaplan A P
出版信息
J Exp Med. 1978 Feb 1;147(2):488-99. doi: 10.1084/jem.147.2.488.
Abstract
Human high molecular weight (HMW) kininogen has been isolated and was found to be a single chain protein of approximately equal to 120,000 daltons. Upon digestion with plasma kallikrein bradykinin is generated, and SDS gel electrophoresis of the kinin-free protein reveals an apparent loss in size of 15,000 daltons. The kinin-free kininogen retains full activity as a coagulation factor and consists of two chains: a heavy chain of approximately equal to 66,000 daltons disulfide-linked to a light chain of 37,000 daltons. The heavy chain of HMW kininogen shares antigenic determinants with LMW kininogen and possesses no detectable coagulant activity. The isolated light chain is shown to be responsible for the coagulant activity of HMW kininogen and contains a unique antigenic determinant that distinguishes HMW kininogen from low molecular weight kininogen.
摘要
人高分子量（HMW）激肽原已被分离出来，发现它是一种单链蛋白质，分子量约为120,000道尔顿。经血浆激肽释放酶消化后可产生缓激肽，对不含激肽的蛋白质进行SDS凝胶电泳显示，其大小明显减少了15,000道尔顿。不含激肽的激肽原作为一种凝血因子保留了全部活性，由两条链组成：一条约66,000道尔顿的重链通过二硫键与一条37,000道尔顿的轻链相连。HMW激肽原的重链与低分子量激肽原具有共同的抗原决定簇，且不具有可检测到的凝血活性。分离出的轻链被证明负责HMW激肽原的凝血活性，并含有一个独特的抗原决定簇，可将HMW激肽原与低分子量激肽原区分开来。
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