An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli
| Autor: | Tiina Immonen, Marja-Leena Laukkanen, Liisa Vanne, Tuula T. Teeri, Kaija Alfthan, Kristiina Takkinen, Matti Kaartinen, Dorothea Sizmann, Jonathan Knowles |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1991 |
| Předmět: |
Protein Denaturation
Glycoside Hydrolases Protein Conformation Recombinant Fusion Proteins Molecular Sequence Data Bioengineering Peptide Enzyme-Linked Immunosorbent Assay Cellulase Biology medicine.disease_cause Biochemistry 03 medical and health sciences 0302 clinical medicine Antibody Specificity medicine Cellulose 1 4-beta-Cellobiosidase Escherichia coli Amino Acid Sequence Molecular Biology 030304 developmental biology chemistry.chemical_classification Trichoderma 0303 health sciences Base Sequence Oxazolone Hydrogen-Ion Concentration biology.organism_classification Enterobacteriaceae 3. Good health Enzyme chemistry Immunoglobulin G biology.protein Antibody Linker Bacteria 030215 immunology Biotechnology |
| Zdroj: | Takkinen, K, Laukkanen, M-L, Sizmann, D, Alfthan, K, Immonen, T, Vanne, L, Kaartinen, M, Knowles, J & Teeri, T 1991, ' An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli ', Protein Engineering, vol. 4, no. 7, pp. 837-841 . https://doi.org/10.1093/protein/4.7.837 |
| ISSN: | 1741-0134 1741-0126 |
| Popis: | 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 IgGl 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/1 of culture medium and its affinity and stability are comparable to those of the corresponding native IgG. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|