title: Refolding chromatography with immobilized mini-chaperones.
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.
authors.affiliation: Cambridge University Chemical Laboratory, Medical Research Council Centre, United Kingdom.
authors.forename: M M
authors.initials: MM
authors.lastname: Altamirano
authors.forename: R
authors.initials: R
authors.lastname: Golbik
authors.forename: R
authors.initials: R
authors.lastname: Zahn
authors.forename: A M
authors.initials: AM
authors.lastname: Buckle
authors.forename: A R
authors.initials: AR
authors.lastname: Fersht
mesh_terms: D018834:Chaperonin 60 / Q000737:chemistry*; D002845:Chromatography / Q000379:methods*; D004926:Escherichia coli; D011489:Protein Denaturation; D017510:Protein Folding
chemical_list: D018834:Chaperonin 60