Recombinant glycoprotein product quality in proliferation-controlled BHK-21 cells
✍ Scribed by Peter P. Mueller; Peter Schlenke; Manfred Nimtz; Harald S. Conradt; Hansjörg Hauser
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 151 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
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 -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 highquality pharmaceutical products and thus warrants further development.
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The effect of different ammonium concentrations and glucosamine on baby hamster kidney (BHK)-21 cell cultures grown in continuously perfused double membrane bioreactors was investigated with respect to the final carbohydrate structures of a secretory recombinant glycoprotein. The human interleukin-2