Csepreghy M, Yeilding A, Lilly M, Hall K, Scott C W, Prchal J T
Division of Hematology/Oncology, University of Alabama, Birmingham 35294.
Am J Hematol. 1988 May;28(1):61-2. doi: 10.1002/ajh.2830280114.
Glucose-6-phosphate-dehydrogenase deficiency is the most common disease-producing enzyme deficiency in man. This paper describes a new glucose-6-phosphate-dehydrogenase variant discovered during the evaluation of an episode of acute hemolytic anemia in a 62-year-old black male, which was temporally related to the ingestion of Tolbutamide. The hemolysis resolved within 10 days despite continuation of Tolbutamide. The erythrocyte glucose-6-phosphate-dehydrogenase activity was significantly decreased, and its electrophoretic mobility was indistinguishable from wild type enzyme, though faster on starch gel with tris, borate, and phosphate buffers. The enzyme had a biphasic pH optimum reduced Km for G-6-P and NADP, decreased utilization of deamino-NADP, and reduced Ki for NADPH. Because the kinetic properties of this enzyme were unique, we have designated it as G6PD Central City.