Expression of properly folded catalytic antibodies in Escherichia coli

J. D. Stewart, I. Lee, B. A. Posner, S. J. Benkovic

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The field of catalytic antibodies has advanced, along with the technology to produce and engineer the proteins. The notion of catalytic antibodies rests on the recognition, first articulated clearly by Linus Pauling, that enzymes owe a large portion of their catalytic power to their ability to bind selectively, and thereby stabilizes the transition state of a reaction to a greater extent than either the reactants or the products. This theory also explained the reason the antibodies should lack such catalytic power, despite the fact that they can strongly and selectively bind virtually any molecule, since they selectively bind to the ground states of molecules. However, if an antibody could be found that selectively bound the transition state for a given reaction, that antibody would possess catalytic power. This chapter discusses the technology to produce and modify these catalysts in bacterial hosts, with an emphasis on producing antibodies in functional form.

Original languageEnglish (US)
Pages (from-to)507-519
Number of pages13
JournalMethods in Enzymology
Volume249
Issue numberC
DOIs
StatePublished - Jan 1 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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