Nagaki K, Hashimoto C, Inai S
Int Arch Allergy Appl Immunol. 1976;50(1):1-13. doi: 10.1159/000231475.
The reaction of C1INA with plasmin was followed by the stoichiometric inactivation of both activities. On acrylamide gel electrophoresis, the reaction mixture revealed 3 new substances. One formed a precipitin band against anti-C1INA and its molecular weight was 103,000 daltons, 14,000 less than that of C1INA, indicating that a portion of C1INA was partially cleaved by the proteolytic activity of plasmin. Each of the other two substances formed precipitin bands against anti-C1INA as well as against anti-plasminogen. Molecular weights of these two substances were 200,000 and 179,000 daltons, whereas the molecular weights of C1INA and plasmin are 117,000 and 82,000 daltons, respectively. From these results, it was concluded that a portion of C1INA in the reaction mixture was partially cleaved by plasmin, and the partially cleaved C1INA as well as the native C1INA form 1:1 molecular complexes with plasmin, leading to inactivation of these activities.
C1INA与纤溶酶反应后，两种活性均按化学计量失活。在丙烯酰胺凝胶电泳中，反应混合物显示出3种新物质。一种物质形成了针对抗C1INA的沉淀带，其分子量为103,000道尔顿，比C1INA的分子量少14,000，表明一部分C1INA被纤溶酶的蛋白水解活性部分切割。另外两种物质中的每一种都形成了针对抗C1INA以及抗纤溶酶原的沉淀带。这两种物质的分子量分别为200,000和179,000道尔顿，而C1INA和纤溶酶的分子量分别为117,000和82,000道尔顿。从这些结果可以得出结论，反应混合物中的一部分C1INA被纤溶酶部分切割，并且部分切割的C1INA以及天然C1INA与纤溶酶形成1:1分子复合物，导致这些活性失活。
