Brzek K
Chair of Biochemistry, Agricultural Academy, Wrocław, Poland.
Acta Biochim Pol. 1987;34(4):431-40.
The activity of glucose dehydrogenase (EC 1.1.1.47; GDH; glucose NAD(P) oxidoreductase) was demonstrated in the supernatant obtained after centrifugation (1500 g) of bovine heart homogenate. More than 50% of GDH activity was found in the microsomal fraction. The optimum pH for the microsomal enzyme was 8.9. About 200-fold purification of GDH was achieved by successive application of ultracentrifugation in 0.25 M mannitol, treatment with solid ammonium sulphate, and CM-32 cellulose chromatography. The purified preparation oxidized not only glucose but also D-glucosamine, N-acetylglucosamine and xylose in 87, 63 and 23%, respectively. Purified GDH was inhibited by p-chloromercuribenzoate and glucose 6-phosphate.
在对牛心匀浆进行离心（1500g）后获得的上清液中证实了葡萄糖脱氢酶（EC 1.1.1.47；GDH；葡萄糖NAD(P)氧化还原酶）的活性。超过50%的GDH活性存在于微粒体部分。微粒体酶的最适pH为8.9。通过在0.25M甘露醇中连续进行超速离心、用固体硫酸铵处理以及CM - 32纤维素色谱法，实现了GDH约200倍的纯化。纯化后的制剂不仅能氧化葡萄糖，还能分别氧化87%的D - 葡糖胺、63%的N - 乙酰葡糖胺和23%的木糖。纯化后的GDH受到对氯汞苯甲酸和6 - 磷酸葡萄糖的抑制。
