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SHR Neuro Krebs Kardio Lipid

Klösch, B; Fürst, W; Kneidinger, R; Schuller, M; Rupp, B; Banerjee, A; Redl, H.
Expression and purification of biologically active rat bone morphogenetic protein-4 produced as inclusion bodies in recombinant Escherichia coli.
Biotechnol Lett. 2005; 27(20):1559-1564
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Abstract:
Rat bone morphogenetic protein-4 (rBMP-4) cDNA was cloned from rat osteoblasts by RT-PCR and expressed in E. coli. Monomeric, dimeric and polymeric forms of recombinant rat BMP-4 (rrBMP-4) were obtained from inclusion bodies after solubilization with urea. The dimer was separated from the remaining polymer and host cell contaminants using size exclusion chromatography. Furthermore, purified rrBMP-4 was stabilized at low urea concentration (40 mM) and at pH 8.5 through the addition of bovine serum albumin. Both, rrBMP-4 dimer and polymer were biologically active as tested by the induction of alkaline phosphatase activity in MC3T3-E1 cells.
Find related publications in this database (using NLM MeSH Indexing)
Animals -
Bone Morphogenetic Proteins - biosynthesis
Cell Line - biosynthesis
Escherichia coli - genetics
Gene Expression - genetics
Inclusion Bodies - genetics
Osteoblasts - metabolism
Rats - metabolism
Recombinant Proteins - biosynthesis

Find related publications in this database (Keywords)
bone morphogenetic protein-4
E. coli
purification
stabilization
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