%0 Journal Article
%T Effects of solvent environment on the structure of hepatitis B surface antigen (HBsAg)<br>溶剂环境对乙肝表面抗原 (HBsAg) 结构的影响
%A Hang Yuan
%A Yan Li
%A Yongdong Huang
%A Jian Luo
%A Guanghui Ma
%A Zhiguo Su
%A <br>原航
%A 李岩
%A 黄永东
%A 罗坚
%A 马光辉
%A 苏志国
%J 生物工程学报
%D 2010
%I 
%X As a virus-like particle, hepatitis B surface antigen (HBsAg) was the primary component of hepatitis B vaccine. HBsAg was maintained by the non-covalent interaction of proteins and lipids. The intact structure of HBsAg particle was vital to its function. However, there was no report about the effects of solvent environment on HBsAg structure. In this paper, we studied the effects of temperature, pH, ionic type and salt concentration on HBsAg structure. The results showed that HBsAg was stable at normal temperature, but began to denature above 60oC. The aggregation of HBsAg at pH 3.0 and 4.0 was nearly irreversible, but partly reversible at pH 5.0. The influence of ionic type on HBsAg was generally in accordance with Hofmeister sequence, except that SO42? caused more aggregation than F?. HBsAg aggregates started to be visible in 0.4 mol/L (NH4)2SO4, and the extent of aggregation increased with the salt concentration. Therefore, caution must be taken when using (NH4)2SO4 in the hydrophobic chromatography purification of HBsAg.
%K HBsAg
%K structural change
%K solvent environment
%K gel filtration-high performance liquid chromatography<br>HBsAg，结构变化，溶剂环境，凝胶过滤高效液相色谱
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=26607D174E01722027CC1215A21EBB60&yid=140ECF96957D60B2&vid=96C778EE049EE47D&iid=59906B3B2830C2C5&sid=C3D6C7213B2FE390&eid=BFDA25D5ECAB4246&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=0