Abstract
Single-chain antibodies consist of the variable, antigen-binding domains of antibodies joined to a continuous polypeptide by genetically engineered peptide linkers. We have used the flexible interdomain linker region of a fungal cellulase to link together the variable domains of an anti-2-phenyloxazolone IgG1 and show here that the resulting single-chain antibody is efficiently secreted and released to the culture medium of Escherichia coli. The yield of affinity-purified single-chain antibody is 1-2 mg/l of culture medium and its affinity and stability are comparable to those of the corresponding native IgG.
Original language | English |
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Pages (from-to) | 837-841 |
Number of pages | 5 |
Journal | PROTEIN ENGINEERING |
Volume | 4 |
Issue number | 7 |
Publication status | Published - Oct 1991 |
MoE publication type | A1 Journal article-refereed |
Keywords
- CELLULASE LINKER PEPTIDE
- ESCHERICHIA-COLI
- EXTRACELLULAR PRODUCTION
- SINGLE-CHAIN ANTIBODY
- VARIABLE DOMAINS
- X-RAY-SCATTERING
- TRICHODERMA-REESEI
- CELLOBIOHYDROLASE-II
- PROTEINS
- GENE
- EXPRESSION
- SEQUENCE
- VECTORS
- FRAGMENT
- PRODUCT