Maleimide as an inhibitor in measurement of erythrocyte glucose-6-phosphate dehydrogenase activity.

Erythrocyte glucose-6-phosphate dehydrogenase activity is measured with a centrifugal analyzer by use of a commercial reagent kit and of the reaction glucose-6-phosphate + NADP+ leads to 6-phosphogluconolactone + NADPH. Rate of production of NADPH is measured and related to hemoglobin concentration. Maleimide is added to inhibit further production of NADPH in a secondary reaction by endogenous 6-phosphogluconate dehydrogenase. The method is compared with others that are designed to circumvent the secondary reaction by either (a) addition of excess phosphogluconate dehydrogenase to drive the secondary reaction to completion or (b) inhibition of endogenous phosphogluconate dehydrogenase by 2,3-diphosphoglycerate. The present method has the advantages that reaction rate more quickly becomes linear and reagent cost is less as compared with other methods. The within-run coefficient of variation was 3%. The various methods investigated showed good statistical correlation.