Science · 1988 · 1.5K citations · 19 references
PharmacyBiochemistryMolecular BiologyAntibody EngineeringMonoclonal AntibodiesProtein EngineeringAntibody CharacterizationAntibody FunctionAntibody PurificationAntibody StructureRecombinant AntibodiesRecombinant Antibody ProductionEscherichia ColiHeavy Chain Variable Region GenesMonoclonal Antibody DesignRecombinant Antibody Technology
Single-chain antigen-binding proteins are novel recombinant polypeptides, composed of an antibody variable light-chain amino acid sequence (VL) tethered to a variable heavy-chain sequence (VH) by a designed peptide that links the carboxyl terminus of the VL sequence to the amino terminus of the VH sequence. These proteins have the same specificities and affinities for their antigens as the monoclonal antibodies whose VL and VH sequences were used to construct the recombinant genes that were expressed in Escherichia coli. Three of these proteins, one derived from the sequence for a monoclonal antibody to growth hormone and two derived from the sequences of two different monoclonal antibodies to fluorescein, were designed, constructed, synthesized, purified, and assayed. These proteins are expected to have significant advantages over monoclonal antibodies in a number of applications.
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James S. Huston, Dennis J. Levinson, M Mudgett-Hunter et al. · Proceedings of the National Academy of Sciences · 1988 · 1.6K citations · Full text
Reshaping human antibodies for therapy
Lutz Riechmann, Herman Waldmann, Greg Winter · Nature · 1988 · 1.6K citations
Replacing the complementarity-determining regions in a human antibody with those from a mouse
Peter Jones, Paul H. Dear, Jefferson Foote et al. · Nature · 1986 · 1.4K citations
Phosphocholine binding immunoglobulin Fab McPC603
Yoshinori Satow, Gerson H. Cohen, Eduardo A. Padlan et al. · Journal of Molecular Biology · 1986 · 572 citations