| Autor: |
Hellebust, H, Uhlén, M, Enfors, S O |
| Zdroj: |
Journal of Bacteriology; September 1990, Vol. 172 Issue: 9 p5030-5034, 5p |
| Abstrakt: |
When a protein derived from the immunoglobulin G (IgG)-binding domains of staphylococcal protein A was expressed in Escherichia coli and recovered from cell extract by IgG affinity chromatography, the 69-kilodalton heat shock protein DnaK was found to be copurified. DnaK could be selectively eluted from the IgG column by ATP or by lowering the pH to 4.7. Protein A could subsequently be eluted by lowering the pH to 3.2. Thus, this procedure allows a one-step purification of both DnaK and protein A from cell extract. In vitro experiments with pure DnaK and protein A revealed that DnaK did not interfere with the IgG-binding properties of protein A but associated with its unfolded C-terminal in a salt-resistant manner. In addition, a specific interaction between DnaK and denaturated casein was found. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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