Expression of glycoprotein-processing enzymes in Escherichia coli as fusion proteins
β Scribed by D.G. Moran; S. Yoshida; K. Fujiyama; T. Seki; T. Yoshida
- Book ID
- 110372807
- Publisher
- Springer
- Year
- 1997
- Tongue
- English
- Weight
- 203 KB
- Volume
- 13
- Category
- Article
- ISSN
- 1573-0972
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π SIMILAR VOLUMES
Many heterologous polypeptides fail to fold into their native state when expressed in Escherichia co~i; instead, they are either degraded by the cellular proteolytic machinery or accumulate in insoluble form, typically as inclusion bodies. Misfolding is a particularly vexing problem in the expressio
Three native E. coli proteins-NusA, GrpE, and bacterioferritin (BFR)-were studied in fusion proteins expressed in E. coli for their ability to confer solubility on a target insoluble protein at the C-terminus of the fusion protein. These three proteins were chosen based on their favorable cytoplasmi