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 in | Applied biochemistry and microbiology Vol. 50; no. 8; pp. 773 - 779 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Moscow
Springer-Verlag
01.12.2014
Pleiades Publishing Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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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. |
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Bibliography: | http://dx.doi.org/10.1134/S0003683814080031 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0003-6838 1608-3024 |
DOI: | 10.1134/S0003683814080031 |