Transport, binding, and polyglutamation of methotrexate in freshly isolated rat hepatocytes.

@article{Gewirtz1980TransportBA,
  title={Transport, binding, and polyglutamation of methotrexate in freshly isolated rat hepatocytes.},
  author={David Gewirtz and J. C. White and Joyce K. Randolph and I. David Goldman},
  journal={Cancer research},
  year={1980},
  volume={40 3},
  pages={573-8}
}
Influx of [3H]methotrexate into freshly isolated hepatocytes in suspension is mediated by two routes, one with a high affinity (Km = 5.9 microM) and another with a low affinity for methotrexate. Both transport routes are equally sensitive to the sulfhydryl group inhibitor, p-chloromercuriphenylsulfonic acid, alterations in temperature, substitution of extracellular Na+ with choline, and inhibition by ouabain or azide. The high-affinity pathway for methotrexate shows specificity for the 4-amino… CONTINUE READING

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