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作 者:许金波[1] 刘育京[1] 李成文[1] 张文福[1] 尤洪涛[1]
机构地区:[1]军事医学科学院微生物流行病研究所
出 处:《中国消毒学杂志》1998年第1期1-5,共5页Chinese Journal of Disinfection
摘 要: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。? Influences of heat on βfolding 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 βfolding configuration, chromophores and peptide bonds of sidechain amino acids of IgG was observed. Only when the exposure time was prolonged to 72 hr, could significant decrease in content of βfolding, 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.
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