Effects of solvent environment on the structure of hepatitis B surface antigen (HBsAg).
- Author:
Hang YUAN
1
;
Yan LI
;
Yongdong HUANG
;
Jian LUO
;
Guanghui MA
;
Zhiguo SU
Author Information
1. National Key Laboratory of Biochemistry Engineering, Chinese Academy of Sciences, Beijing 100190, China.
- Publication Type:Journal Article
- MeSH:
Ammonium Sulfate;
chemistry;
Hepatitis B Surface Antigens;
chemistry;
Hepatitis B Vaccines;
chemistry;
Hepatitis B virus;
chemistry;
Hydrogen-Ion Concentration;
Protein Denaturation;
Solvents;
Temperature
- From:
Chinese Journal of Biotechnology
2010;26(12):1674-1682
- CountryChina
- Language:Chinese
-
Abstract:
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 60 degrees C. 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 SO4(2-) 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.
