Refolding chromatography with immobilized mini-chaperones

Myriam M. Altamirano, Ralph Golbik, Ralph Zahn, Ashley M. Buckle, Alan R. Fersht

Research output: Contribution to journalArticleResearchpeer-review

126 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3576-3578
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number8
DOIs
Publication statusPublished - 15 Apr 1997
Externally publishedYes

Keywords

  • folding
  • GroEL
  • hsp60
  • protein
  • renaturation

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