伴随人哈格曼因子酶促激活的结构变化
Structural changes accompanying enzymatic activation of human Hageman factor.
作者信息
Revak S D, Cochrane C G, Johnston A R, Hugli T E
出版信息
J Clin Invest. 1974 Sep;54(3):619-27. doi: 10.1172/JCI107799.
Abstract
The structure of Hageman factor, isolated from human plasma, was analyzed before and after enzymatic activation. The purified molecule is a single polypeptide chain of 80,000 molecular weight (mol wt) sedimenting at 4.5S. An amino acid analysis has been performed. The concentration of Hageman factor in normal human plasma was found to be 29 mug/ml with variation between individuals ranging from 15 to 47 mug/ml. Treatment of the molecule with kallikrein, plasmin, or trypsin resulted in cleavage at two primary sites, yielding fragments of 52,000, 40,000, and 28,000 mol wt. No further changes occurred in the fragments with subsequent reduction. Prekallikrein-activating ability was associated exclusively with the 28,000 moiety.
摘要
对从人血浆中分离出的哈格曼因子在酶促激活前后的结构进行了分析。纯化后的分子是一条分子量为80,000的单多肽链，沉降系数为4.5S。已进行了氨基酸分析。发现正常人血浆中哈格曼因子的浓度为29微克/毫升，个体间差异范围为15至47微克/毫升。用激肽释放酶、纤溶酶或胰蛋白酶处理该分子会导致在两个主要位点发生裂解，产生分子量为52,000、40,000和28,000的片段。随后还原时，这些片段未发生进一步变化。前激肽释放酶激活能力仅与28,000的部分相关。
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