Document Detail

Refolding chromatography with immobilized mini-chaperones.
MedLine Citation:
PMID:  9108018     Owner:  NLM     Status:  MEDLINE    
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.
M M Altamirano; R Golbik; R Zahn; A M Buckle; A R Fersht
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  94     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1997 Apr 
Date Detail:
Created Date:  1997-05-22     Completed Date:  1997-05-22     Revised Date:  2013-04-16    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3576-8     Citation Subset:  IM    
Cambridge University Chemical Laboratory, Medical Research Council Centre, United Kingdom.
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MeSH Terms
Chaperonin 60 / chemistry*
Chromatography / methods*
Escherichia coli
Protein Denaturation
Protein Folding*
Reg. No./Substance:
0/Chaperonin 60

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