Purification of bone morphogenetic protein-2 from refolding mixtures using mixed-mode membrane chromatography View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-01

AUTHORS

Gesa Gieseler, Iliyana Pepelanova, Lena Stuckenberg, Louis Villain, Volker Nölle, Uwe Odenthal, Sascha Beutel, Ursula Rinas, Thomas Scheper

ABSTRACT

In this study, we present the development of a process for the purification of recombinant human bone morphogenetic protein-2 (rhBMP-2) using mixed-mode membrane chromatography. RhBMP-2 was produced as inclusion bodies in Escherichia coli. In vitro refolding using rapid dilution was carried out according to a previously established protocol. Different membrane chromatography phases were analyzed for their ability to purify BMP-2. A membrane phase with salt-tolerant properties resulting from mixed-mode ligand chemistry was able to selectively purify BMP-2 dimer from refolding mixtures. No further purification or polishing steps were necessary and high product purity was obtained. The produced BMP-2 exhibited a biological activity of 7.4 × 105 U/mg, comparable to commercial preparations. Mixed-mode membrane chromatography can be a valuable tool for the direct purification of proteins from solutions with high-conductivity, for example refolding buffers. In addition, in this particular case, it allowed us to circumvent the use of heparin-affinity chromatography, thus allowing the design of an animal-component-free process. More... »

PAGES

123-130

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00253-016-7784-1

DOI

http://dx.doi.org/10.1007/s00253-016-7784-1

DIMENSIONS

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PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27542381


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