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- W2073018439 abstract "Abstract We describe the properties of a dihydrofolate reductase purified from lymphoblastoid cells which acquired methotrexate resistance following long-term culture in presence of the drug. The enzyme showed marked differences in kinetic properties from the parental cell strain. The K m for dihydrofolate was increased 18 -fold, relative to the parent line, and the affinity of the enzyme for methotrexate was decreased by 50 -fold. Binding of NADPH, however, was tighter than in the parent line, with a K m of less than half the original value. The molecular weight of the mutant dihydrofolate reductase, as measured by gel filtration, was unaltered, but the mutant enzyme showed much greater heat lability than the wild-type enzyme. At low drug concentrations, cells possessing the altered reductase possessed a selective advantage over cells with normal dihydrofolate reductase. Increasing the selective pressure, however, by raising the methotrexate concentration in the medium above 1·6 × 10 −6 M, led to selection against the mutant, and cells with normal type dihydrofolate reductase again dominated the populalation. These results are interpreted in the context of high-affinity and low-affinity sites of action of methotrexate." @default.
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- W2073018439 date "1977-06-01" @default.
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- W2073018439 title "Acquired methotrexate resistance in lymphoblasts resulting from altered kinetic properties of dihydrofoltate reductase" @default.
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- W2073018439 doi "https://doi.org/10.1016/0014-2964(77)90118-9" @default.
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