Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3356541 | Immunology Letters | 2006 | 6 Pages |
Abstract
The single chain variable fragment (scFv) of an anti-idiotypic catalytic monoclonal antibody, 9G4H9, displaying a β-lactamase-like activity was cloned. The recombinant protein was expressed through the periplasm in Escherichia coli in the presence or in the absence of FkpA, a chaperone-like enzyme and tested for its hydrolytic activity. The results show that the catalytic parameters for hydrolysis of ampicillin by scFv9G4H9 are clearly influenced by the presence of FkpA, indicating that the correct folding of the fragment represents a crucial step for catalysis.
Related Topics
Life Sciences
Immunology and Microbiology
Immunology
Authors
Séverine Padiolleau-Lefèvre, Hélène Débat, Denis Phichith, Daniel Thomas, Alain Friboulet, Bérangère Avalle,