Kurdi-Haidar B, Luzzatto L
Department of Haematology, Royal Postgraduate Medical School, London, U.K.
Mol Biochem Parasitol. 1990 Jun;41(1):83-91. doi: 10.1016/0166-6851(90)90099-8.
Glucose-6-phosphate dehydrogenase (G6PD) from Plasmodium falciparum has been detected previously in cultures of parasites grown in G6PD-deficient red blood cells. Using polyacrylamide gel electrophoresis, a semi-quantitative assay has been developed to compare the level of the parasite enzyme activity in G6PD normal and in G6PD-deficient host cells. The results do not support the previous contention that the host cell G6PD-deficiency necessarily affects the level of expression of the parasite enzyme. The plasmodial enzyme was partially purified from extracts of parasites prepared by digitonin lysis of infected red blood cells, and its distinctive biochemical properties are described. P. falciparum G6PD has a KmG6P of 27 microM, a KmNADP of 4.5 microM, and KiNADPH of 4.5 microM, indicating an affinity for all its main ligands much higher than that of normal human red cell G6PD.
此前在缺乏葡萄糖-6-磷酸脱氢酶（G6PD）的红细胞中培养的恶性疟原虫培养物中已检测到该酶。利用聚丙烯酰胺凝胶电泳，已开发出一种半定量测定法，以比较在G6PD正常和G6PD缺乏的宿主细胞中寄生虫酶活性的水平。结果不支持先前的论点，即宿主细胞G6PD缺乏必然会影响寄生虫酶的表达水平。通过对感染红细胞进行洋地黄皂苷裂解制备的寄生虫提取物中部分纯化了疟原虫酶，并描述了其独特的生化特性。恶性疟原虫G6PD的6-磷酸葡萄糖（KmG6P）为27微摩尔，烟酰胺腺嘌呤二核苷酸磷酸（KmNADP）为4.5微摩尔，烟酰胺腺嘌呤二核苷酸磷酸（KiNADPH）为4.5微摩尔，表明其对所有主要配体的亲和力远高于正常人红细胞G6PD。
