Increased yield of high purity recombinant human brain natriuretic peptide by acid hydrolysis of short fusion partner in Escherichia coli

•Developed a strategy to clone and express rhBNP as inclusion bodies with acid cleavage site.•Optimized a simple purification method that yields greater purity and quantity of rhBNP.•This method could be an alternative method of choice for production of small therapeutic peptides. Recombinant human...

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Veröffentlicht in:	Protein expression and purification 2015-07, Vol.111, p.61-67
Hauptverfasser:	Kanumuri, Radha Madhavi, Bajji, Chitra, Tummuru, Rajesh R., Tatireddigari, Venkat R.R. Arva, Mangamoori, Lakshmi Narasu, Panati, Kalpana, Narala, Venkata Ramireddy
Format:	Artikel
Sprache:	eng
Schlagworte:	Acid hydrolysis B-type natriuretic peptide Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli - metabolism Fusion protein Humans Hydrolysis Inclusion body Natriuretic Peptide, Brain - biosynthesis Natriuretic Peptide, Brain - chemistry Natriuretic Peptide, Brain - genetics Natriuretic Peptide, Brain - isolation & purification Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - isolation & purification Reversed phase chromatography
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