热力对IgG分子构象影响的研究

经圆二色光谱和紫外差光谱分析，冻干ＩｇＧ经８０℃作用２ｈ后，其β 折叠构象及侧链氨基酸生色基团和肽键未见明显变化。作用时间延长至７２ｈ，β 折叠含量则明显减少，氨基酸生色基团和肽键的紫外最大吸收波长蓝移，分子变构。溶液中的ＩｇＧ经６０℃处理１０ｈ后也有一定程度的变构。

STUDY ON INFLUENCE OF HEAT ON MOLECULAR CONFIGURATION OF IgG

? Influences of heat on β folding configurations, chromophores and peptide bonds of amino acids of IgG were observed experimentally using circular dichroism (CD) spectrometry and ultraviolet differential spectrometry. The results indicated that when lyophilized IgG was exposed to 80℃ heat for 2 hr, no significant change in β folding configuration, chromophores and peptide bonds of side chain amino acids of IgG was observed. Only when the exposure time was prolonged to 72 hr, could significant decrease in content of β folding, blue shift of maximal absorption wave length of chromophores and peptide bonds of amino acids and change in molecular configuration be seen. When IgG in solution was exposed to 60℃ heat for 10 hr or 80℃ heat for 5 min, certain change in configuration of IgG occurred.