Refolding and purification of the huGM-CSF(9-127)-IL-6(29-184) fusion protein / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 291-294, 2002.
Article
Dans Chinois
| WPRIM
| ID: wpr-231332
ABSTRACT
The huGM-CSF(9-127)-IL-6(29-184) fusion protein was precipitated on column when being purified by Q Sepharose H.P. ion exchange chromatography after renaturation by dilution. To solve this problem, a novel purification and refolding strategy was adopted. Inclusion bodies was first purified by Q Sepharose H.P. ion exchange in 8 mol/L urea, followed by in situ refolding on column by Sephacryl S-200. Renatured fusion protein was obtained in a purity of more than 95%. It was showed that the method of refolding on gel filtration column is efficient, with relative refolding rate at 80%. By the whole procedure, refolding and purification of recombinant protein can be performed within one day. This strategy is also promising to be applied in large scale purification and refolding of recombinant protein from inclusion bodies in E. coli.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Fragments peptidiques
/
Protéines de fusion recombinantes
/
Chimie
/
Facteur de stimulation des colonies de granulocytes et de macrophages
/
Interleukine-6
/
Pliage des protéines
langue:
Chinois
Texte intégral:
Chinese Journal of Biotechnology
Année:
2002
Type:
Article
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