Literature DB >> 9108018

Refolding chromatography with immobilized mini-chaperones.

M M Altamirano1, R Golbik, R Zahn, A M Buckle, A R Fersht.   

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.

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Year:  1997        PMID： 9108018      PMCID： PMC20481          DOI： 10.1073/pnas.94.8.3576

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  15 in total

1.  Secondary structure of Escherichia coli glucosamine-6-phosphate deaminase from amino acid sequence and circular dichroism spectroscopy.

Authors:  M M Altamirano; J A Plumbridge; A Hernández-Arana; M Calcagno
Journal:  Biochim Biophys Acta       Date:  1991-01-29

2.  Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution.

Authors:  K Braig; P D Adams; A T Brünger
Journal:  Nat Struct Biol       Date:  1995-12

3.  Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.

Authors:  R Zahn; A M Buckle; S Perrett; C M Johnson; F J Corrales; R Golbik; A R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  1996-12-24       Impact factor: 11.205

4.  Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

Authors:  A Buchberger; H Schröder; T Hesterkamp; H J Schönfeld; B Bukau
Journal:  J Mol Biol       Date:  1996-08-23       Impact factor: 5.469

5.  Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.

Authors:  J A Mendoza; B Demeler; P M Horowitz
Journal:  J Biol Chem       Date:  1994-01-28       Impact factor: 5.157

6.  Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.

Authors:  Y Makino; H Taguchi; M Yoshida
Journal:  FEBS Lett       Date:  1993-12-27       Impact factor: 4.124

7.  Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.

Authors:  G Oliva; M R Fontes; R C Garratt; M M Altamirano; M L Calcagno; E Horjales
Journal:  Structure       Date:  1995-12-15       Impact factor: 5.006

8.  Chemical coupling of peptides and proteins to polysaccharides by means of cyanogen halides.

Authors:  R Axén; J Porath; S Ernback
Journal:  Nature       Date:  1967-06-24       Impact factor: 49.962

9.  Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation, and to promote protein folding.

Authors:  H Taguchi; Y Makino; M Yoshida
Journal:  J Biol Chem       Date:  1994-03-18       Impact factor: 5.157

10.  [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides].

Authors:  G Fischer; H Bang; C Mech
Journal:  Biomed Biochim Acta       Date:  1984
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  18 in total

1.  The substrate binding domain of DnaK facilitates slow protein refolding.

Authors:  Naoki Tanaka; Shota Nakao; Hiromasa Wadai; Shoichi Ikeda; Jean Chatellier; Shigeru Kunugi
Journal:  Proc Natl Acad Sci U S A       Date:  2002-11-14       Impact factor: 11.205

2.  High-throughput automated refolding screening of inclusion bodies.

Authors:  Renaud Vincentelli; Stéphane Canaan; Valérie Campanacci; Christel Valencia; Damien Maurin; Frédéric Frassinetti; Loréna Scappucini-Calvo; Yves Bourne; Christian Cambillau; Christophe Bignon
Journal:  Protein Sci       Date:  2004-10       Impact factor: 6.725

3.  A novel system for continuous protein refolding and on-line capture by expanded bed adsorption.

Authors:  Henrik Ferré; Emmanuel Ruffet; Lise-Lotte B Nielsen; Mogens Holst Nissen; Timothy J Hobley; Owen R T Thomas; Søren Buus
Journal:  Protein Sci       Date:  2005-08       Impact factor: 6.725

4.  The MitCHAP-60 disease is due to entropic destabilization of the human mitochondrial Hsp60 oligomer.

Authors:  Avital Parnas; Michal Nadler; Shahar Nisemblat; Amnon Horovitz; Hanna Mandel; Abdussalam Azem
Journal:  J Biol Chem       Date:  2009-08-25       Impact factor: 5.157

5.  GroEL-GroES-mediated protein folding requires an intact central cavity.

Authors:  J D Wang; M D Michelitsch; J S Weissman
Journal:  Proc Natl Acad Sci U S A       Date:  1998-10-13       Impact factor: 11.205

6.  The allosteric mechanism of the chaperonin GroEL: a dynamic analysis.

Authors:  J Ma; M Karplus
Journal:  Proc Natl Acad Sci U S A       Date:  1998-07-21       Impact factor: 11.205

Review 7.  Chaperonins.

Authors:  N A Ranson; H E White; H R Saibil
Journal:  Biochem J       Date:  1998-07-15       Impact factor: 3.857

8.  Human CD1d-glycolipid tetramers generated by in vitro oxidative refolding chromatography.

Authors:  A Karadimitris; S Gadola; M Altamirano; D Brown; A Woolfson; P Klenerman; J L Chen; Y Koezuka; I A Roberts; D A Price; G Dusheiko; C Milstein; A Fersht; L Luzzatto; V Cerundolo
Journal:  Proc Natl Acad Sci U S A       Date:  2001-03-13       Impact factor: 11.205

9.  Design of highly stable functional GroEL minichaperones.

Authors:  Q Wang; A M Buckle; N W Foster; C M Johnson; A R Fersht
Journal:  Protein Sci       Date:  1999-10       Impact factor: 6.725

10.  In vivo activities of GroEL minichaperones.

Authors:  J Chatellier; F Hill; P A Lund; A R Fersht
Journal:  Proc Natl Acad Sci U S A       Date:  1998-08-18       Impact factor: 11.205
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