Optimization Of The Preparation Process Of Single-Chain Antibody And Lidamycin Prosthetic Protein Fusion Protein
Keywords
Inclusion Bodies, Type Iv Collagenase, Fusion Protein, Purification, Renaturation
Abstract
Optimize the preparation process of the anti-type IV collagenase single-chain antibody and lidamycin prosthetic protein fusion protein fv-ldp expressed in the form of inclusion bodies. Optimize its inclusion body preparation and dissolution, immobilized metal chelation chromatography and step-by-step dialysis renaturation process through single factor or orthogonal design, finely purify the protein through sephadexg-75 chromatography, and detect its inclusion body based on saturation binding experiment using flow cytometry. Antigen binding activity. After optimization, the purity of fv-ldp inclusion bodies was 63.9% and the solubility was 95.7%; after purification, the purity of fv-ldp reached more than 95%, the monomer content after renaturation accounted for 60%, and after fine purification, it increased to 85%, which was higher than the initial recombination. The sexual condition is increased by 5.6 times, and it can bind to human lung adenocarcinoma PAA cells and liver cancer bel-7402 cells. The preparation process of fv-ldp has been successfully optimized, laying an experimental foundation for its production and research and development, and also providing a more practical method for the preparation of other miniaturized antibody drugs based on single-chain antibodies expressed in the form of inclusion bodies.
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Original research was done by Gao Ruijuan, Zhao Chunyan, Li Diandong, Zhen Yongsu
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