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 trim
Regulatory mutants of dihydrofolate reductase in Escherichia coli K12
โ Scribed by Sheldon, Robert ;Brenner, Sydney
- Publisher
- Springer
- Year
- 1976
- Tongue
- English
- Weight
- 668 KB
- Volume
- 147
- Category
- Article
- ISSN
- 0026-8925
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โฆ Synopsis
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 reductase is regulatdd by a diffusible molecule, and is probably under negative control. The regulatrory mutants, some of which are temperature-sensitive, act cis.
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