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Selected Publication:

Mueller, PP; Schlenke, P; Nimtz, M; Conradt, HS; Hauser, H.
Recombinant glycoprotein product quality in proliferation-controlled BHK-21 cells.
Biotechnol Bioeng. 1999; 65(5):529-536 Doi: 10.1002/(SICI)1097-0290(19991205)65:5<529::AID-BIT5>3.0.CO;2-M
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Co-authors Med Uni Graz
Schlenke Peter
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Abstract:
We analyzed product quality to determine the applicability of proliferation-controlled mammalian cells for recombinant pharmaceutical protein production. Baby hamster kidney (BHK)-21 cells were engineered to express a dicistronic, stabilized, self-selecting growth control system consisting of a beta-estradiol-activatable transcription factor IRF-1 fusion protein. IRF-1 activity led to a reduced growth rate, whereas productivity, protein integrity, and glycosylation pattern of the industrially relevant secreted pharmaceutical glycoprotein erythropoietin remained consistent, showing that this technique has the potential for improving the consistency of high-quality pharmaceutical products and thus warrants further development.
Find related publications in this database (using NLM MeSH Indexing)
Animals -
Biotechnology -
Carbohydrate Sequence -
Cell Division -
Cell Line -
Cricetinae -
DNA-Binding Proteins - genetics
Erythropoietin - genetics Erythropoietin - isolation & purification Erythropoietin - standards
Glycoproteins - biosynthesis Glycoproteins - standards
Glycosylation -
Humans -
Interferon Regulatory Factor-1 -
Molecular Sequence Data -
Oligosaccharides - chemistry Oligosaccharides - isolation & purification
Phosphoproteins - genetics
Protein Engineering -
Quality Control -
Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - standards

Find related publications in this database (Keywords)
proliferation control
recombinant human erythropoietin glycosylation
baby hamster kidney (BHK) cells
IRF-1
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