Correct disulfide pairing and efficient refolding of detergent-solubilized single-chain Fv proteins from bacterial inclusion bodies
- 1 December 1995
- journal article
- Published by Elsevier in Molecular Immunology
- Vol. 32 (17-18) , 1443-1452
- https://doi.org/10.1016/0161-5890(95)00105-0
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Mammalian Cell Expression of Single–Chain Fv (sFv) Antibody Proteins and Their C–terminal Fusions with Interleukin–2 and Other Effector DomainsNature Biotechnology, 1994
- Refolding Recombinant Proteins: Process Strategies and Novel ApproachesAnnals of the New York Academy of Sciences, 1994
- Renaturation, Purification and Characterization of Recombinant Fab-Fragments Produced in Escherichia coliNature Biotechnology, 1991
- A comparison of strategies to stabilize immunoglobulin Fv-fragmentsBiochemistry, 1990
- A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxinNature, 1989
- Single-Chain Antigen-Binding ProteinsScience, 1988
- Properties of inclusion bodies from recombinant Escherichia coliBiochemical Society Transactions, 1988
- Removal of sodium dodecyl sulfate from proteins and peptides by gel filtrationAnalytical Biochemistry, 1981
- Removing unbound detergent from hydrophobic proteinsAnalytical Biochemistry, 1980
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959