Gahr M, Schröter W, Sturzenegger M, Bornhalm D, Marti H R
Helv Paediatr Acta. 1976 Aug;31(2):159-66.
A new variant of erythrocytic glucose-6-phosphate dehydrogenase has been found in a family of Swiss origin. It is associated with chronic nonsphaerocytic haemolytic anaemia. The enzyme from the erythrocytes of a young boy of this family was partially purified 110-fold and characterized. It revealed reduced catalytic activity, increased thermolability and two maxima of the pH activity curve at pH 7.0 and 8.5. The Km value for glucose-6-phosphate was reduced, that for NADP was normal. The enzyme showed an increased inhibitor constant for NADPH with respect to NADP. Electrophoretic mobility was normal (B+). 2-Desoxyglucose-6-phosphate and galactose-6-phosphate were utilized at normal rates, whereas the analogue deamino-NADP gave an increased utilization rate. The mother of the propositus could be identified as heterozygous for this enzyme deficiency. Chronic haemolysis is possibly due to the increased thermolability of the variant enzyme.
在一个瑞士裔家庭中发现了一种红细胞葡萄糖-6-磷酸脱氢酶的新变体。它与慢性非球形红细胞溶血性贫血有关。对该家庭一名小男孩红细胞中的酶进行了110倍的部分纯化并进行了特性鉴定。结果显示其催化活性降低、热稳定性增加,且pH活性曲线在pH 7.0和8.5处有两个峰值。葡萄糖-6-磷酸的Km值降低,NADP的Km值正常。该酶对NADPH的抑制常数相对于NADP增加。电泳迁移率正常(B+)。2-脱氧葡萄糖-6-磷酸和半乳糖-6-磷酸的利用率正常,而类似物脱氨基-NADP的利用率增加。先证者的母亲可被鉴定为该酶缺乏的杂合子。慢性溶血可能是由于变体酶热稳定性增加所致。