Kleniewski J, Donaldson V H, Wagner C J
Thromb Res. 1982 Mar 1;25(5):387-99. doi: 10.1016/0049-3848(82)90129-3.
When purified human HMW-kininogen was digested by plasmin, its specific antigenic properties were initially enhanced and then gradually destroyed, but its clot-promoting activity (Fitzgerald factor activity) was only slightly decreased. When endogenous serum plasminogen was activated by streptokinase, similar alterations in specific HMW-kininogen antigens and Fitzgerald factor activity occurred. In contrast, trypsin induced increased antigenic properties initially, but readily destroyed the Fitzgerald factor activity and less readily destroyed the specific HMW-kininogen antigenic properties in purified HMW-kininogen and in normal human serum. When normal serum was treated with streptokinase, the antigenic properties shared by HMW and LMW-kininogens were in Sephadex G-200 fractions of lower molecular weight than in the case of untreated serum, but the elution volumes of specific HMW-kininogen antigens and Fitzgerald factor activity were not significantly altered. When prekallikrein-deficient serum was subjected to the same G-200 gel filtration process, there was a broad overlap in the elution volumes of antigens shared by both HMW and LMW-kininogens with specific HMW-kininogen antigenic and coagulant properties, which remained after streptokinase treatment of the serum. Depsite the disparate rates of destruction of the antigenic and clot-promoting portion of HMW-kininogen by proteases these properties did not separate from one another during ion exchange chromatography.
当纯化的人高分子量激肽原被纤溶酶消化时，其特异性抗原特性最初增强，然后逐渐被破坏，但其促凝活性（菲茨杰拉德因子活性）仅略有下降。当内源性血清纤溶酶原被链激酶激活时，高分子量激肽原特异性抗原和菲茨杰拉德因子活性也会发生类似变化。相比之下，胰蛋白酶最初会使抗原特性增加，但会迅速破坏菲茨杰拉德因子活性，并且在纯化的高分子量激肽原和正常人血清中较不容易破坏高分子量激肽原的特异性抗原特性。当用链激酶处理正常血清时，高分子量和低分子量激肽原共有的抗原特性在葡聚糖凝胶G-200分离组分中的分子量比未处理血清的情况更低，但高分子量激肽原特异性抗原和菲茨杰拉德因子活性的洗脱体积没有明显改变。当将前激肽释放酶缺乏的血清进行相同的葡聚糖凝胶G-200凝胶过滤过程时，高分子量和低分子量激肽原共有的抗原与高分子量激肽原特异性抗原和凝血特性在洗脱体积上有广泛重叠，这些特性在血清经链激酶处理后仍然存在。尽管蛋白酶对高分子量激肽原的抗原和促凝部分的破坏速率不同，但在离子交换色谱过程中这些特性并未彼此分离。
