An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli |
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| Authors: | Takkinen, Kristiina Laukkanen, Marja-Leena Sizmann, Dorothea Alfthan, Kaija Immonen, Tiina Vanne, Liisa Kaartinen, Matti Knowles, Jonathan K.C. Teeri, Tuula T. |
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| Affiliation: | VTT Biotechnical Laboratory PO Box 202, SF-02151 Espoo 1Department of Bacteriology and Immunology, University of Helsinki SF-00290 Helsinki, Finland |
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| Abstract: | Single-chain antibodies consist of the variable, antigen-bindingdomains of antibodies joined to a continuous polypeptide bygenetically engineered peptide linkers. We have used the flexibleinterdomain linker region of a fungal cellulase to link togetherthe variable domains of an anti-2-phenyloxazolone IgGl and showhere that the resulting single-chain antibody is efficientlysecreted and released to the culture medium of Escherichia coli.The yield of affinity-purified single-chain antibody is 1 -2mg/1 of culture medium and its affinity and stability are comparableto those of the corresponding native IgG. |
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| Keywords: | cellulase linker peptide/ Escherichia coli/ extracellular production/ single-chain antibody/ variable domains |
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