Summary
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 regulatory mutations occur in the structural gene for dihydrofolate reductase.
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Communicated by W. Arber
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Sheldon, R. Altered dihydrofolate reductase in fol regulatory mutants of Escherichia coli K12. Molec. gen. Genet. 151, 215–219 (1977). https://doi.org/10.1007/BF00338697
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DOI: https://doi.org/10.1007/BF00338697