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HBsAg作为乙肝疫苗的主要成分,是一种病毒样颗粒,由蛋白质和脂类通过非共价键作用形成。HBsAg保持完整结构对其功能非常重要,而目前未见对其在溶液中结构变化的研究。考察了不同溶剂环境(温度、pH值、离子类型和盐浓度)对HBsAg结构的影响。实验发现,HBsAg在常温下比较稳定,但在温度超过60℃时稳定性明显下降;pH值小于4.0时引起不可逆聚集,但在pH5.0时的聚集部分可逆;不同离子对HBsAg的影响基本符合Hofmeister序列,不同之处是SO42-比F-更易引起HBsAg颗粒的聚集,在所考察的盐中,(NH4)2SO4对HBsAg有着较大的影响,0.4mol/L时就会引起HBsAg聚集,随着浓度增加,聚集现象更加严重,所以在HBsAg的疏水层析中要谨慎使用(NH4)2SO4。
As a major component of hepatitis B vaccine, HBsAg is a virus-like particle formed by the non-covalent interaction of proteins and lipids. It is very important for HBsAg to maintain its intact structure to its function, but no study on its structural changes in solution has been found so far. The effects of different solvent environments (temperature, pH value, ionic type and salt concentration) on the structure of HBsAg were investigated. It was found that the stability of HBsAg was stable at room temperature, but its stability decreased obviously when the temperature was over 60 ℃. When the pH value was less than 4.0, irreversible aggregation was caused, but the aggregation was reversible at pH 5.0. The effect of different ions on HBsAg was basically consistent Hofmeister sequence, except that SO42- is more likely to cause the aggregation of HBsAg particles than F-. In the salts examined, (NH4) 2SO4 has a large effect on HBsAg, and at 0.4mol / Concentration increases, the aggregation phenomenon is more serious, so the hydrophobic chromatography of HBsAg should be used with caution (NH4) 2SO4.