Display Settings:

Format

Send to:

Choose Destination
Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3576-8.

Refolding chromatography with immobilized mini-chaperones.

Author information

  • 1Cambridge University Chemical Laboratory, Medical Research Council Centre, United Kingdom.

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.

PMID:
9108018
[PubMed - indexed for MEDLINE]
PMCID:
PMC20481
Free PMC Article

Images from this publication.See all images (1)Free text

Figure 1
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk