Order of Fusions between Bacterial and Mammalian Proteins Can Determine Solubility inEscherichia coli
- 1 March 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 244 (3) , 933-937
- https://doi.org/10.1006/bbrc.1998.8365
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Solubility of Proteins Isolated from Inclusion Bodies Is Enhanced by Fusion to Maltose-Binding Protein or ThioredoxinProtein Expression and Purification, 1998
- Free luciferase may acquire a more favorable conformation than ribosome‐associated luciferase for its activity expressionFEBS Letters, 1997
- Recombination of protein domains facilitated by co-translational folding in eukaryotesNature, 1997
- Folding of an Enzyme into an Active Conformation While Bound as Peptidyl-tRNA to the RibosomeBiochemistry, 1995
- The Preparation of Catalytically Active Human Cathepsin B from Its Precursor Expressed in Escherichia coli in the Form of Inclusion BodiesEuropean Journal of Biochemistry, 1995
- Release of Proteins and Peptides from Fusion Proteins Using a Recombinant Plant Virus ProteinaseAnalytical Biochemistry, 1994
- A T7 expression vector for producing N- and C-terminal fusion proteins with glutathione S-transferaseGene, 1994
- The high‐resolution crystal structure of porcine pepsinogenProteins-Structure Function and Bioinformatics, 1992
- The Structure and Function of the Aspartic ProteinasesAnnual Review of Biophysics, 1990
- Expression and Refolding of Recombinant Human Fibroblast Procathepsin DDNA and Cell Biology, 1990