NDLI: Recombinant protein production using the Semliki Forest Virus expression system

Content Provider	Springer Nature Link
Author	Blasey, H.D. Lundström, K. Tate, S. Bernard, A.R.
Copyright Year	1997
Abstract	We report here the successful scale up of transient recombinant protein expression to litre scale using Semliki Forest Virus System. The expression of bacterial β-galactosidase was initially compared in BHK and CHO cells and the conditions for optimal infection of BHK cells were identified. 10% FCS in a medium at pH 6.9 and infection in small volumes were found to be optimal. A high MOI results in an increased recombinant protein yield. Stirring does not affect the infection process. Finally we applied these optimal conditions to the production of a microsomal enzyme, human cyclooxygenase-2 in suspension spinners. Five independant productions at the 1 litre scale yielded reproducible substantial amounts of recombinant protein (16 mg microsomal protein 109 cells−1) with an average specific activity of 3942 ± 765 pg PGE2 μg−1 microsomal protein 5 min−1.
Starting Page	65
Ending Page	72
Page Count	8
File Format	PDF
ISSN	09209069
Journal	Cytotechnology
Volume Number	24
Issue Number	1
e-ISSN	15730778
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1997-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biomedicine general Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Clinical Biochemistry Bioengineering Biomedical Engineering Biotechnology

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Recombinant protein production using the Semliki Forest Virus expression system