10 mM isatin (2,3-dioxoindole) inhibited glucose influx into human erythrocytes by over 30%. The inhibition is of the competitive type, where the affinity constant (Kt) was increased from 5.71 (control) to 11.11 mM in the presence of isatin with no change in Vmax (130 nmol/min/ml packed cells). The observed inhibition of sugar transport by isatin was not mediated through membrane -SH groups accessible to iodoacetate, iodoacetamide, DTNB, DNP or sodium arsenite. Isatin inhibited sugar transport in the presence of 2 mM harmaline, an alkaloid inhibitor of Na+, K(+)-ATPase activity. The inhibition was non additive which suggests that these two compounds interact with the same or a similar site on the erythrocyte membrane.