Turner A J, Whittle S R, Hryszko J, Guha S R
J Neurochem. 1982 Aug;39(2):306-9. doi: 10.1111/j.1471-4159.1982.tb03947.x.
Reductase activity towards two aldose substrates has been examined in subcellular fractions prepared from rat brain. The reduction of glucuronate, which is sensitive to inhibition by the anticonvulsant drug sodium valproate, corresponds to the major high-Km aldehyde reductase in brain. Xylose reduction that is insensitive to valproate inhibition has characteristics consistent with the activity of aldose reductase (EC 1.1.1.21). Both enzymes are predominantly localized in the cytosolic fraction. The significance of the location of these two reductases is discussed in relation to the compartmentation of catecholamine metabolism in brain.
已在从大鼠脑制备的亚细胞组分中检测了对两种醛糖底物的还原酶活性。葡萄糖醛酸的还原对抗惊厥药物丙戊酸钠的抑制敏感，它对应于脑中主要的高Km醛还原酶。对丙戊酸抑制不敏感的木糖还原具有与醛糖还原酶（EC 1.1.1.21）活性一致的特征。这两种酶主要定位于胞质组分中。结合脑中儿茶酚胺代谢的区室化讨论了这两种还原酶定位的意义。
