Tanahashi T, Tochikubo K, Hachisuka Y
Jpn J Microbiol. 1976 Aug;20(4):281-6. doi: 10.1111/j.1348-0421.1976.tb00989.x.
Glucose-6-phosphate dehydrogenase [D-glucose-6-phosphate: NADP oxidoreductase, EC. 1. 1. 1. 49] obtained from spores of Bacillus subtilis PCI 219 strain was partially purified by filtration on Sephadex G-200, ammonium sulfate fractionation and chromatography on DEAE-Sephadex A-25 (about 54-fold). The optimum pH for stability of this enzyme was about 6.3 and the optimum pH for the reaction about 8.3. The apparent Km values of the enzyme were 5.7 X 10(-4) M for glucose-6-phosphate and 2.4 X 10(-4) M for nicotinamide adenine dinucleotide phosphate (NADP). The isoelectric point was about pH 3.9. The enzyme activity was unaffected by the addition of Mg++ or Ca++. The inactive glucose-6-phosphate dehydrogenase obtained from the spores heated at 85 C for 30 min was not reactivated by the addition of ethylenediaminetetraacetic acid, dipicolinic acid or some salts unlike inactive glucose dehydrogenase.
从枯草芽孢杆菌PCI 219菌株的孢子中获得的葡萄糖-6-磷酸脱氢酶[D-葡萄糖-6-磷酸：NADP氧化还原酶，EC. 1. 1. 1. 49]，通过在Sephadex G-200上过滤、硫酸铵分级分离以及在DEAE-Sephadex A-25上进行色谱分离（约54倍）进行了部分纯化。该酶稳定性的最适pH约为6.3，反应的最适pH约为8.3。该酶对葡萄糖-6-磷酸的表观Km值为5.7×10⁻⁴ M，对烟酰胺腺嘌呤二核苷酸磷酸（NADP）的表观Km值为2.4×10⁻⁴ M。其等电点约为pH 3.9。酶活性不受添加Mg²⁺或Ca²⁺的影响。与失活的葡萄糖脱氢酶不同，从在85℃加热30分钟的孢子中获得的失活葡萄糖-6-磷酸脱氢酶，添加乙二胺四乙酸、二吡啶甲酸或某些盐后不会重新激活。
