IgG的β-折叠构象变化对其生物学活性的影响

Influence of β-fold Structure on Biological Activity of IgG

采用圆二色谱和Westernblot等方法观察了热处理后冻于兔疫球蛋白G（IgG）的结构及生物学活性变化。经80℃72h和100℃2h干热处理后，IgG的β－折叠发生变构，活性抗原量减少，抗原决定簇有改变，抗体难以识别抗原，说明IgG的β－折叠构象改变对其生物学活性有明显的影响。

The changes of β-fold structure and biological activity of freeze--dried IgGafter heat treatment was studied by circular dichroism spectrometer and Western blot. Theresult showed that, after being heated at 80℃ for 72h or 100℃ for 2h, both the β-fold structureand antigen deterdrinant of IgG were changed, and the amount of active antigen wasdecreased, so the antigen was difficult to be recognized by antibody. It demonstrated that thebiological activity of IgG was significantly influenced by the change of β-fold structure of it.