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Evidence from temperature studies that the human erythrocyte hexose transporter has a transient memory of its dissociated ligands

The inhibition constant of L‐sorbose efflux (Ki(sorbose)) from human erythrocytes for inhibition by D‐glucose increases from 5.15 +/− 0.89 to 12.24 +/− 1.9 mM on cooling from 50 degrees C to 30 degrees C; the Ki(sorbose) of D‐mannose increases similarly on cooling. The activation energy Ea(sorbose) of net L‐sorbose exit from human erythrocytes is 62.9 +/− 3.1 kJ mol‐1; but in the co‐presence of 5 mM D−glucose Ea(sorbose) is reduced to 41.7 +/− 1.6 kJ mol‐1 (P < 0.005). These data are consistent with the view that when D‐glucose binds to the hexose transporter it leads to an activated transporter state which remains transiently activated after glucose dissociates; if L‐sorbose binds to the excited state it is more mobile than otherwise and consequently the apparent Ki(sorbose) of D‐glucose is raised. Cooling prolongs the decay time of the activated state; hence the Ki(sorbose) of D‐glucose rises as temperature is reduced.