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 an...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites, Antibody
- Cattle
- Cysteine
- Disulfides
- Escherichia coli
- Immunoglobulin Fragments
- Immunoglobulin Variable Region
- Mice
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Plasmids
- Protein Conformation
- Recombinant Fusion Proteins
- Structure-Activity Relationship