Optimization of the refolding of recombinant human granulocyte-macrophage colony-stimulating factor immobilized on affinity sorbent

A method for the production and purification of biologically active recombinant human granulocyte-macrophage colony-stimulating factor (rhGM-CSF), expressed in Escherichia coli, has been developed. Washing of an inclusion body fraction which allows the removal of numerous ballast proteins and on-col...

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Published inApplied biochemistry and microbiology Vol. 50; no. 8; pp. 773 - 779
Main Authors Kosobokova, E. N, Skrypnik, K. A, Pinyugina, M. V, Shcherbakov, A. I, Kosorukov, V. S
Format Journal Article
LanguageEnglish
Published Moscow Springer-Verlag 01.12.2014
Pleiades Publishing
Springer Nature B.V
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Summary:A method for the production and purification of biologically active recombinant human granulocyte-macrophage colony-stimulating factor (rhGM-CSF), expressed in Escherichia coli, has been developed. Washing of an inclusion body fraction which allows the removal of numerous ballast proteins and on-column refolding of rhGM-CSF are specific characteristics of the method. The refolding efficiency reached 70%; the purity of the preparation constituted 95%. The biological activity was similar to those of other recombinant hGM-CSF analogs.
Bibliography:http://dx.doi.org/10.1134/S0003683814080031
ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683814080031