Structural requirements for binding to the sugar-transport system of the human erythrocyte.

@article{Barnett1973StructuralRF,
  title={Structural requirements for binding to the sugar-transport system of the human erythrocyte.},
  author={Jerald E Barnett and Geoffrey D Holman and Kenneth A. Munday},
  journal={The Biochemical journal},
  year={1973},
  volume={131 2},
  pages={
          211-21
        }
}
The structural requirements for binding to the glucose/sorbose-transport system in the human erythrocyte were explored by measuring the inhibition constants, K(i), for specifically substituted analogues of d-glucose when l-sorbose was the penetrating sugar. Derivatives in which a hydroxyl group in the d-gluco configuration was inverted, or replaced by a hydrogen atom, at C-1, C-2, C-3, C-4 or C-6 of the d-glucose molecule, all bound to the carrier, confirming that no single hydroxyl group is… CONTINUE READING
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