Refolding chromatography with immobilized mini-chaperones
Open Access
- 15 April 1997
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 94 (8) , 3576-3578
- https://doi.org/10.1073/pnas.94.8.3576
Abstract
Mini-chaperones (e.g., a peptide consisting of residues 191-345 of GroEL) that are immobilized on agarose have very efficient chaperoning activity with several proteins that are otherwise recalcitrant to renaturation by conventional methods. We have used immobilized mini-chaperones both in column chromatography and batchwise to renature an insoluble protein from an inclusion body, to refold apparently irreversibly denatured proteins, and to recondition enzymes that have lost activity on storage. Refolding chromatography offers an efficient and simple means to renature proteins in high yield and with biological activity.Keywords
This publication has 15 references indexed in Scilit:
- Chaperone activity and structure of monomeric polypeptide binding domains of GroELProceedings of the National Academy of Sciences, 1996
- Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein FoldingJournal of Molecular Biology, 1996
- Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 å resolutionStructure, 1995
- Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolutionNature Structural & Molecular Biology, 1995
- Inactive GroEL Monomers Can Be Isolated and Reassembled to Functional Tetradecamers That Contain Few Bound PeptidesJournal of Biological Chemistry, 1995
- High Hydrostatic Pressure Induces the Dissociation of cpn60 Tetradecamers and Reveals a Plasticity of the MonomersJournal of Biological Chemistry, 1995
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATPFEBS Letters, 1993
- Secondary structure of Escherichia coli glucosamine-6-phosphate deaminase from amino acid sequence and circular dichroism spectroscopyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Chemical Coupling of Peptides and Proteins to Polysaccharides by Means of Cyanogen HalidesNature, 1967