We report the identification and characterization of a novel degradation product associated with PEGylation of a recombinant protein. After several months of storage at 2 β’ C-8 β’ C, an unexpected increase was observed in the proportion of an impurity that eluted with the native unPEGylated protein b
Production of a recombinant protein in a silkworm
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 44 KB
- Volume
- 106
- Category
- Article
- ISSN
- 0006-3592
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β¦ Synopsis
The silkworm synthesizes large amounts of silk proteins in its silk glands and spins them into silk fibers to build a cocoon. This ability to synthesize silk proteins in large quantities may be useful for the mass production of recombinant proteins. In this issue of B&B, Adachi and coworkers have succeeded in synthesizing a large amount of recombinant human collagen a chain (the non-triple helical a1 chain of human type I collagen) using a transgenic silkworm. They tested the possibility of using the collagen a chain as a cell culture scaffold, and found that cells could be cultured on the chain as on marketed gelatin-the denatured and fragmented form of collagen. Since the collagen a chain has uniform molecular weight and no risks of animal-derived pathogen contamination, the a chain is a promising candidate biomaterial as a high-quality and safe substitute for marketed gelatin.
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