Article
The disulfide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in Escherichia coli.
Biochemistry - 11 Feb 1992
Glockshuber R, Schmidt T, Plückthun A
Abstract excerpt
The formation of the disulfide bonds in the variable domains VH and VL of the antibody McPC603 was found to be essential for the stability of all antigen binding fragments investigated. Exposure of the Fv fragment to reducing conditions in vitro resulted in irreversible denaturation of both VH and VL. In vitro refolding of the reduced Fv fragment was only possible when the disulfide bonds were allowed to form...
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