A fluorescence study of substrate and inhibitor binding to bovine liver dihydrofolate reductase.

@article{Degan1989AFS,
  title={A fluorescence study of substrate and inhibitor binding to bovine liver dihydrofolate reductase.},
  author={Paolo Degan and P. Carpano and Giovanni Cercignani and G Montagnoli},
  journal={The International journal of biochemistry},
  year={1989},
  volume={21 3},
  pages={291-5}
}
1. Covalent coupling of fluorescein to methotrexate (MTX) by a 5-carbon spacer yields a dihydrofolate reductase (DHFR) inhibitor (FMTX) with Ki = 11 nM. 2. FMTX shows a fluorescence quenching with respect to fluorescein which is relieved by binding to the enzyme. 3. The dissociation constants (Kd) of MTX, FMTX, NADPH and 7,8-dihydrofolate (DHF) from bovine liver DHFR have been determined by fluorometric titrations. 4. The Kd values for NADPH, MTX and FMTX from the complementary binary complexes… CONTINUE READING
0 Citations
0 References
Similar Papers

Similar Papers

Loading similar papers…