Evidence from studies of temperature-dependent changes of D-glucose, D-mannose and L-sorbose permeability that different states of activation of the human erythrocyte hexose transporter exist for good and bad substrates.

@article{Naftalin1997EvidenceFS,
  title={Evidence from studies of temperature-dependent changes of D-glucose, D-mannose and L-sorbose permeability that different states of activation of the human erythrocyte hexose transporter exist for good and bad substrates.},
  author={Richard J. Naftalin},
  journal={Biochimica et biophysica acta},
  year={1997},
  volume={1328 1},
  pages={
          13-29
        }
}
  • Richard J. Naftalin
  • Published 1997
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • (1) The inhibition constant of L-sorbose flux from fresh human erythrocytes by D-glucose, Ki(sorbose) increases on cooling from 50 degrees C to 30 degrees C from 5.15 +/- 0.89 mM to 12.24 +/- 1.9 mM; the Ki(sorbose) of D-mannose increases similarly, indicating that the process is endothermic. (2) The activation energy Ea(sorbose) of net L-sorbose exit is 62.9 +/- 3.1 kJ/mol; in the co-presence of 5 mM D-glucose Ea(sorbose) is reduced to 41.7 +/- 1.6 kJ/mol (P < 0.005). (3) Cooling from 35… CONTINUE READING