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Article Abstract
The large protein of hepatitis B virus surface antigen (LHBs) contained an attachment site of HBV to liver cells and the antibodies to preS1 were virus-neutralizing. Therefore, vaccines containing preS1 would be more protective. However, One of the key problems in the preparation of gene-expressed proteins was the purification of the products. We have established a method of immuno-affinity chromatography with the anti-HBsAg-preS1 monoclonal antibody. Using this technique, We have successfully purified gene-expressed fusion protein of hepatitis B virus surface antigen containing preS1 (21-47). Results showed that this method was simple, effective and specific as compared to other methods, and might be useful in the future.
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