将抗ＨＢｓＡｇ 抗体的轻链（Ｌ）和重链Ｆｄ 段基因，分别克隆于ｐＥＴ２０ｂ 质粒中并分别转化到大肠肝菌ＢＬ２１（ＤＥ３），ＬＰＴＧ诱导后，ＳＤＳ－ＰＡＧＥ分析发现在２７ＫＤ（Ｌ）和２５ＫＤ（Ｆｄ）处有外源蛋白表达，表达蛋白含量分别为５３％ 和４８％ 。Ｌ链和Ｆｄ 包涵体蛋白经盐酸胍变性后，等量混合于折叠液中，Ｌ和Ｆｄ 可复性形成了约５０ＫＤ的蛋白。ＥＬＩＳＡ结果表明，复性蛋白具有与ＨＢｓＡｇ 结合的能力。抗ＨＢｓＡｇ 抗体Ｆａｂ 段在大肠杆菌中的表达与复性的成功，表明包涵体表达基因工程抗体在技术是可行的。 The light chain (L) and heavy chain Fd fragment of anti-HBsAg antibody were cloned into pET20b plasmid and transformed into E. coli BL21 (DE3) respectively. After induced by LPTG, SDS- The foreign protein was expressed at 25KD (Fd), the expressed protein content was 53% and 48% respectively. L chain and Fd inclusion body protein denatured by guanidine hydrochloride, the same amount of mixed in the folding fluid, L and Fd can be refolded to form a protein of about 50KD. ELISA results showed that renatured proteins have the ability to bind to HBsAg. The successful expression and refolding of anti-HBsAg Fab in Escherichia coli showed that it is feasible to express the engineered antibody in inclusion bodies.