Engineering N-glycosylation pathways in the baculovirus-insect cell system
โ Scribed by Donald L Jarvis; Ziad S Kawar; Jason R Hollister
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 548 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0958-1669
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โฆ Synopsis
The inability to produce eukaryotic glycoproteins with complex N-linked glycans is a major limitation of the baculovirus-insect cell expression system. Recent studies have demonstrated that metabolic engineering can be used to extend the glycoprotein processing capabilities of lepidopteran insect cells. This approach is being used to develop new baculovirus-insect cell expression systems that can produce more authentic recombinant glycoproteins and obtain new information on insect N-glycosylation pathways.
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In order to develop an efficient process for large-scale production of recombinant protein, various factors were studied which affect the productivity of Sf-9 (Spodoptera frugiperda) insect cells when using the baculovirus expression system. It was shown that upon infection with the Bac-BRV6L recomb
## Abstract The cell density effect (i.e., the drop in the specific productivity in the baculovirusโinsect cells expression system when cells are infected at high cell densities) has been extensively described in the literature. In this article, a model for the central metabolism of serumโfree susp
The properties of Sf9 and Tn5 insect cells were analyzed comparatively under serum-free culture conditions. Sf9 cells in SF90011 medium apparently utilized sucrose as a primary nutrient both before and after virus infection, yielding small amounts of lactate and ammonia. Tn5 cells in Excell 401 medi
## Abstract Glycosylation has profound effects on the quality of recombinant proteins produced in mammalian cells. The biosynthetic pathways of Nโlinked glycans on glycoproteins involves a relatively small number of enzymes and nucleotide sugars. Many of these glycoconjugate enzymes can utilize mul
## Abstract Bradykinin exerts its actions via binding to B~1~ and B~2~ receptors (B~1~R and B~2~R), which are members of G proteinโcoupled receptor superfamily. B~2~R is constitutively expressed in a variety of cells such as endothelial cells, vascular smooth muscle cells, and cardiomyocytes and it