FORMATION AND STRUCTURE OF HUMAN HAGEMAN-FACTOR FRAGMENTS
FORMATION AND STRUCTURE OF HUMAN HAGEMAN-FACTOR FRAGMENTS
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DOI：
10.1172/jci110656
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发表时间：
1982-01-01
影响因子：
15.9
通讯作者：
KAPLAN, AP
中科院分区：
文献类型：
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作者：
DUNN, JT;KAPLAN, AP
活化的Hageman因子（HFa）的自动消化产生了40，000-MW的活化酶以及Hageman因子片段（HFf）; HFf由28，500和30，000的2种MW物质组成。研究了这些活性片段的结构，还原后，每个片段具有28，000的H链。通过使碘化蛋白质进行二维平板凝胶电泳来鉴定相关的L链，其中第二维是还原的。40，000-道尔顿的酶具有15，000的L链，30，000-道尔顿形式的HFf具有2000的L链;与28，500-道尔顿形式的HFf相关的L链的证据（推定的MW约500)有人建议。30，000-道尔顿形式的HFf先于28，500形式。天然HF消化形成HFa明显先于裂解，裂解使分子片段化并降低其MW。HFa的28，500-道尔顿L链成为每个片段化产物的H链，而在沿HFa H链的沿着不同点的裂解决定将产生哪些片段。HFa的激肽释放酶消化主要产生HFf;然而，当前激肽释放酶缺陷（弗莱彻性状）血浆被激活时，可以看到40，000-道尔顿酶。
Autodigestion of activated Hageman factor (HFa) yielded a 40,000-MW activated enzyme as well as Hageman factor fragment (HFf); HFf consisted of 2 MW species of 28,500 and 30,000. The structure of these active fragments was investigated and, upon reduction, each possessed a H chain of 28,000. The associated L chains were identified by subjecting iodinated proteins to 2-dimensional slab gel electrophoresis in which the 2nd dimension was run reduced. The 40,000-dalton enzyme had a L chain of 15,000, and the 30,000-dalton form of HFf had a L chain of 2000; evidence of a L chain associated with the 28,500-dalton form of HFf (putative MW .apprx. 500) was suggested. The 30,000-dalton form of HFf preceded the 28,500 form. Digestion of native HF to form HFa evidently preceded cleavages that fragment the molecule and diminish its MW. The 28,500-dalton L chain of HFa became the H chain of each of the fragmentation products while cleavage at different points along the H chain of HFa determined which fragments will be produced. Kallikrein digestion of HFa yielded primarily HFf; however, the 40,000-dalton enzyme may be seen when prekallikrein-deficient (Fletcher trait) plasma is activated.