Abstract
The core antigen of the hepatitis B virus (HBcAg) has been used widely as a diagnostic reagent for the identification of the viral infection. However, purification using the conventional sucrose density gradient ultracentrifugation is time consuming and costly. To overcome this, HBcAg particles displaying His-tag on their surface were constructed and produced in Escherichia coli. The recombinant His-tagged HBcAgs were purified using immobilized metal affinity chromatography. Transmission electron microscopy and enzyme-linked immunosorbent assay (ELISA) revealed that the displayed His-tag did not impair the formation of the core particles and the antigenicity of HBcAg. © 2009 Elsevier B.V. All rights reserved.
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Yap, W. B., Tey, B. T., Ng, M. Y. T., Ong, S. T., & Tan, W. S. (2009). N-terminally His-tagged hepatitis B core antigens: Construction, expression, purification and antigenicity. Journal of Virological Methods, 160(1–2), 125–131. https://doi.org/10.1016/j.jviromet.2009.04.038
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