Masuda K
Jpn J Med Sci Biol. 1983 Feb;36(1):39-41. doi: 10.7883/yoken1952.36.39.
Each of the three major components isolated from a commercial plasmin-treated human immunoglobulin preparation, namely, the plasmin-resistant 7S IgG fraction (PRG), Fab fragment and Fc fragment, was tested before and after heat treatment for binding C1q and fixing C3bi. In unheated state, only PRG was found to bind C1q, whereas none bound C3bi. The binding of C1q by PRG was enhanced by heat treatment which also conferred the activity of binding C3bi to PRG and to Fc fractions, From these results, anticomplementary activity of unheated PRG fraction seems to be due mainly to the complement activation via the classical pathway, whereas the activation by the heat-treated Fc fragment might be via an alternative pathway.
从市售的经纤溶酶处理的人免疫球蛋白制剂中分离出的三种主要成分，即抗纤溶酶的7S IgG组分（PRG）、Fab片段和Fc片段，在热处理前后均进行了结合C1q和固定C3bi的测试。在未加热状态下，仅发现PRG能结合C1q，而没有一种能结合C3bi。热处理增强了PRG对C1q的结合能力，同时也赋予了PRG和Fc组分结合C3bi的活性。根据这些结果，未加热的PRG组分的抗补体活性似乎主要归因于通过经典途径的补体激活，而热处理后的Fc片段的激活可能是通过替代途径。
