| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3407426 | Journal of Virological Methods | 2009 | 7 Pages |
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.
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Authors
Wei Boon Yap, Beng Ti Tey, Michelle Y.T. Ng, Swee Tin Ong, Wen Siang Tan,