Conformation of high molecular weight kininogen: effects of kallikrein and factor XIa cleavage.
Conformation of high molecular weight kininogen: effects of kallikrein and factor XIa cleavage.
复制标题
高分子量激肽原的构象：激肽释放酶和 XIa 因子裂解的影响。
DOI：
10.1016/s0006-291x(89)80178-0
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发表时间：
1989
影响因子：
3.1
通讯作者：
Colman,RW
中科院分区：
文献类型：
--
作者：
Villanueva,GB;Leung,L;Bradford,H;Colman,RW
研究了激肽释放酶和因子XIa对高分子量激肽原（HK）蛋白水解的影响。圆二色性（CD）光谱表明，裂解HK血浆激肽释放酶或尿激肽释放酶，这两个结果在一个积极的辅因子（HKa），结果在构象变化，其特征在于在222 nm处的CD椭圆率增加。这表明有组织的二级结构增加。相比之下，由因子XIa切割HK导致无活性辅因子（HKi），其特征在于在222 nm处CD椭圆率急剧降低，表明完全不同类型的构象变化。HK的固有荧光增强后，由所有三种蛋白酶切割。这些构象变化可能在决定HKa和HKi的结构和功能中起作用。
The effect of kallikrein and factor XIa proteolysis of high molecular weight kininogen (HK) was investigated. Circular dichroism (CD) spectroscopy showed that cleavage of HK by plasma kallikrein or urinary kallikrein, both of which result in an active cofactor (HKa), results in conformational change that is characterized by increase in CD ellipticity at 222 nm. This suggests an increase in organized secondary structures. By contrast, cleavage of HK by factor XIa which results in an inactive cofactor (HKi) is characterized by a dramatic decrease in CD ellipticity at 222 nm suggesting an entirely different type of conformational change. The intrinsic fluorescence of HK is enhanced after cleavage by all three proteases. These conformational changes may play a role in determining the structure and function of HKaand HKi.