| TECHNOLOGY |
Most proteins moth > 2 disulfides couldn't be expressed in active form in any significant amount. Instead they end up as insoluble, misfolded proteins. The researchers mutated Escherichia coli bacteria, creating modified organisms whose cytoplasm is highly oxidizing. Researchers's previous work some years ago; developed E. coli mutants in which the cytoplasm's thioredoxin (reducing agent) was impaired, permitting the cytoplasm to become oxidizing which normally stabilizes disulfide bonds. The new study shows that by improving earlier original mutants the cytoplasm can be rendered very oxidizing so that protein folding is more efficient The researchers also introduce into the cytoplasm, via a plasmid a protein that shuffles disulfide bonds when they are incorrectly formed The researchers demonstrated the technique on 4 model proteins - Bacterial alkaline phosphatase - Mouse Urokinase - Human tissue plasminogen activator's short fragment - Human tissue plasminogen activator In all 4 cases the result was appreciable yields of active protein |
| UPDATE | 12.99 |
| AUTHOR | This data is not available for free |
| LITERATURE REF. | This data is not available for free |
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