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J. Biochem, 2003, Vol. 134, No. 6 813-817
© 2003 Japanese Biochemical Society

MOLECULAR BIOLOGY

Expression, Purification, and Characterization of Humanized Anti-HBs Fab Fragment

Deng Ning*,1, Xiang Junjian1, Wang Xunzhang2, Chen Wenyin3, Zhang Qing2, Su Kuanyuan3, Rao Guirong3, Ren Xiangrong3, Long Qingxin2 and Yu Zhouyao3

1 Life Science and Technology College in Jinan University, Guangzhou, 510632, China; 2 Life Science College in Zhongshan University, Guangzhou, 510275, China; and 3 The Central Research Institute, 458th Hospital of PLA, Guangzhou, 510602, China

Anti-HBs Fab fragment has considerable potential for use in the prevention and treatment of liver diseases by HBV. Here we established a high-level expression system to directly produce anti-HBs Fab fragment in Pichia pastoris. This was achieved by co-integration of the genes encoding the heavy and light chains both under the genome of the yeast cells. The Fab fragment was efficiently secreted into medium at a concentration of 50 mg/liter. The authenticity of the Fab fragment was confirmed by immunoblot analysis, which yielded one band of ~50 kDa under nonreducing conditions and two bands of ~28 kDa under reducing conditions. The anti-HBs Fab fragment was prepared with a purity of 95% by affinity chromatography. The affinity activity of the recombinant Fab was detected by ELISA, which indicated that 1 mg of recombinant Fab was equivalent to 40 IU HBIG (20 IU/mg). The results demonstrated that the recombinant Fab fragment could sufficiently neutralize the HBsAg.

* Corresponding author: Life Science and Technology College in Jinan University, Guangzhou, 510632, China. Email: dengning123{at}sohu.com


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