Abstract
The effect of disulfides on glycolysis in human erythrocytes has been studied. High concentrations of cystamine and cystamine derivatives inhibit the utilization of glucose, whereas utilization of adenosine or inosine is unaffected. The inhibitory effect on glycolysis has been ascribed to a block at the hexokinase level. This block cannot be explained by a depletion of the ATP of the cells. The "disulfide poisoning" can be reversed with adenosine or by treatment with thiols. The possibility of a reversible mixed disulfide formation involving thiol groups of hexokinase is discussed.