<p><b>OBJECTIVE</b>To study the effect of
gene optimization on the expression and purification of HDV small
antigen produced by
genetic engineering.</p><p><b>
METHODS</b>Based on the
colon preference of E. coli, the HDV small
antigen original
gene from
GenBank was optimized. Both the original
gene and the optimized
gene expressed in
prokaryotic cells,
SDS-PAGE was made to analyze the
protein expression yield and to decide which
protein expression style was more proportion than the other. Furthermore, two
antigens were purified by
chromatography in order to compare the purity by
SDS-PAGE and Image Lab
software.</p><p><b>RESULTS</b>
SDS-PAGE indicated that the
molecular weight of target
proteins from two groups were the same as we expected.
Gene optimization resulted in the higher yield and it could make the product more soluble. After
chromatography, the purity of target
protein from optimized
gene was up to 96.3%, obviously purer than that from original
gene.</p><p><b>CONCLUSION</b>
Gene optimization could increase the
protein expression yield and
solubility of
genetic engineering HDV small
antigen. In addition, the product from the optimized
gene group was easier to be purified for
diagnosis usage.</p>