Multiple forms of L1210 dihydrofolate reductase differing in affinity for methotrexate.

@article{Duffy1984MultipleFO,
  title={Multiple forms of L1210 dihydrofolate reductase differing in affinity for methotrexate.},
  author={T. Duffy and S. Beckman and F. M. Huennekens},
  journal={Biochemical and biophysical research communications},
  year={1984},
  volume={119 1},
  pages={
          352-8
        }
}
Dihydrofolate reductase, purified from a Methotrexate-resistant subline (R6) of L1210 mouse leukemia cells, consists of two forms (designated 1 and 2) differing in affinity for the drug. Form 1 is more sensitive to inhibition by Methotrexate. Form 2 is more heat-labile, but it can be stabilized by bovine serum albumin or NADPH. Isoelectric focusing resolves 1 and 2; pI values are 7.4 and 8.2. Forms 1 and 2 comprise about 10 and 90% of the total protein, but 1 has at least a 2-fold higher… Expand
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