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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1991 May 1;88(9):4001–4004. doi: 10.1073/pnas.88.9.4001

Construction and characterization of a single-chain catalytic antibody.

R A Gibbs 1, B A Posner 1, D R Filpula 1, S W Dodd 1, M A Finkelman 1, T K Lee 1, M Wroble 1, M Whitlow 1, S J Benkovic 1
PMCID: PMC51581  PMID: 2023948

Abstract

The antigen-binding (Fab) fragment of the catalytic monoclonal antibody NPN43C9 has recently been cloned by using bacteriophage lambda. By inserting the variable regions of this Fab coding sequence into a (NH2)-VL-linker-VH-(COOH) construct (where VL and VH represent the heavy and light chain variable regions), we have assembled a recombinant gene encoding a catalytic single-chain antigen-binding protein. This protein has been expressed in Escherichia coli and exhibits the same catalytic parameters as the parent monoclonal antibody NPN43C9. Single-chain forms of catalytic antibodies may prove valuable for structural and site-directed mutagenesis studies as well as for large-scale applications of catalytic antibodies.

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Selected References

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