Trimethoprim inhibits dihydrofolate reductase. Mutations conferring trimethorpim-resistance on E coli K12 result in either an altered reductase with decreased affinity for the drug, or in 2-30 fold higher levels of the enzyme. Studies of the latter class of mutants indicate that dihydrofolate reduct
Altered dihydrofolate reductase in fol regulatory mutants of Escherichia coli K12
โ Scribed by Sheldon, Robert
- Publisher
- Springer
- Year
- 1977
- Tongue
- English
- Weight
- 414 KB
- Volume
- 151
- Category
- Article
- ISSN
- 0026-8925
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โฆ Synopsis
Three spontaneous fol regulatory mutants contain dihydrofolate reductase molecules which differ in physical properties from enzymes of their parent strains. The enzymes were purified over 100-fold by affinity chromatography and were shown to differ in vitro in thermolability and in affinity for trimethoprim, a competitive inhibitor of the enzyme. These results indicate that some fol regulatroy mutations occur in the structural gene for dihydrofolate reductase.
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