Isolation of chimaeric forms of elongation factor EF-Tu by affinity chromatography
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12013219
DOI
10.1016/s0378-4347(01)00525-4
PII: S0378434701005254
Knihovny.cz E-resources
- MeSH
- Chromatography, Affinity methods MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Peptide Elongation Factor Tu isolation & purification MeSH
- Recombinant Fusion Proteins isolation & purification MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Peptide Elongation Factor Tu MeSH
- Recombinant Fusion Proteins MeSH
Six different recombinant chimaeric forms of a three-domain protein, proteosynthetic elongation factor Tu (EF-Tu), composed of domains of EF-Tu of mesophilic (Escherichia coli) and thermophilic (Bacillus stearothermophilus) origin as well as free N-terminal domains of EF-Tu, and the whole recombinant EF-Tus of both organisms were prepared and isolated by the GST (glutathione S-transferase) fusion technology. Several modifications in the standard isolation and purification procedures are described that proved necessary to obtain the proteins in a purified and undegraded form.
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