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《ACTA BIOCHIMICA ET BIOPHYSICA SINICA》 1999-05
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Construction and Expression of hTNFα h TGF 3 Fused Gene

CHEN Jian Jun, SUN Miao, LU Fang, CHEN Chang Qing CHEN Jian Jun, SUN Miao, LU Fang, CHEN Chang Qing CHEN Jian Jun, SUN Miao, LU Fang, CHEN Chang Qing * and WANG De Bao 1 ( Shanghai Research Center of Biotechnology, the Chinese Acad  
Human tumor necrosis factor was fused with hTGF3, the third loop region of hTGFα specifically binding to EGF receptor, through a flexible linker by recombinant DNA techniques. The constructed plasmid containing h TNF α h TGF 3 fused gene, pSB92 TLT , was expressed under the control of P L promoter and after the induction at 42 ℃ it gave a high level of expression of the fused gene, ranging in 50%—60% of total bacterial protein. 95% of the expressed product was inclusion body, and only 5% was soluble. When the fused gene was constructed into the constitutive plasmid pLC, a new plasmid controlled by P L promoter but without cIts 857, and expressed at 30 ℃, the expression yield reached 50% and a high proportion of soluble protein, 35% of total bacterial protein, was obtained. Western blot analysis indicated that the fusion protein could specifically bind to anti hTNFα antibody. Comparing to original hTNFα, the fused hTNFα derivative showed about equal cytotoxicity to L929 cell line and higher cytotoxicity to some human tumor cell lines. This shows that the fusion protein TLT may be promising in application.
【Fund】: 国家高技术“863”计划资助项目
【CateGory Index】: Q786
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