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目的 :探讨IVIG在 6 0℃、10h灭活病毒过程中 ,木糖醇和低 pH对于生成低ACAIgG聚体的作用。 方法 :利用高压液相、荧光光谱、圆二色谱、紫外吸收光谱以及IgG聚体对木瓜酶水解敏感性的差别来确定IgG聚体的空间构象及维持IgG聚体的价键变化。结果 :木糖醇及低pH的条件下加热导致IgG折叠趋于紧密 ,维持IgG聚体的价键增多 ,热稳定性增强 ,但其聚体的补体结合位点不易被C1大分子靠近亲和。相反 ,在无稳定剂存在时 ,6 3℃、2 0min、pH7.4的条件下加热导致IgG折叠趋于松散 ,其补体结合位点有利于C1大分子靠近亲和 ,相应的聚体激活补体的能力较强。结论 :IVIG在加热灭活病毒中 ,木糖醇和低 pH极大地降低了IgG聚体的生成及其ACA ,适宜的稳定剂和 pH的选择是制备高质量IVIG制品的重要环节。
OBJECTIVE: To investigate the effect of xylitol and low pH on the generation of low ACAIgG in IVIG at 60 ℃ and 10h inactivation of virus. Methods: The spatial conformation of IgG aggregates and the valence bond changes of IgG aggregates were determined by HPLC, fluorescence spectroscopy, circular dichroism spectroscopy, UV-vis absorption spectra and the sensitivity of IgG aggregates to papain hydrolysis. Results: Under the condition of xylitol and low pH, the IgG folding tended to be close, and the valence bond of IgG aggregates was increased and the thermostability was enhanced. However, the complement binding sites of the aggregates were not easy to get close to the affinity of C1 macromolecules . In contrast, heating in the absence of a stabilizing agent at 6 3 ° C, 20 min, pH 7.4 resulted in the looseness of the IgG folds, with the complement binding sites favoring the close proximity of C1 macromolecules and the corresponding aggregates activating complement Strong ability. Conclusion: IVIG heat inactivated virus, xylitol and low pH greatly reduce the formation of IgG aggregates and ACA, the choice of suitable stabilizers and pH is an important part of the preparation of high quality IVIG products.