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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 structure and biological activities of rabbit IgG immunoglobulin G after heat treatment were observed by circular dichroism and Western blot. After 80 ℃ 72h and 100 ℃ 2h dry heat treatment, the β-sheet of IgG is disaggregated, the amount of active antigen is reduced, the antigenic determinant is changed, the antibody is difficult to recognize antigen, which indicates that the change of β-sheet conformation of IgG changes its biological activity Have a clear impact.