Zhang T M, Giroix M H, Sener A, Malaisse W J
Laboratory of Experimental Medicine, Erasmus Medical School, Brussels Free University, Belgium.
Biochem Mol Biol Int. 1994 Aug;33(6):1127-33.
UDP-glucose pyrophosphorylase was measured in rat pancreatic islets, the generation of D-glucose 1-phosphate from UDP-glucose and PPI being eventually coupled to the generation of L-[U-14C]glutamate from 14C-labelled alpha-ketoglutarate. The activity of the enzyme was about one order of magnitude lower in islet than liver homogenates. The affinity of the enzyme for either UDP-glucose or PPi was comparable, however, in liver and islets. The activity of UDP-glucose pyrophosphorylase was somewhat lower in islets from animals with inherited or acquired diabetes mellitus than in those from control rats. These findings are considered in connection with the accumulation of glycogen in islets of hyperglycemic animals.
在大鼠胰岛中测定了UDP - 葡萄糖焦磷酸化酶,由UDP - 葡萄糖和焦磷酸生成D - 葡萄糖1 - 磷酸最终与由14C标记的α - 酮戊二酸生成L - [U - 14C]谷氨酸相偶联。该酶在胰岛中的活性比肝脏匀浆中的活性低约一个数量级。然而,该酶对UDP - 葡萄糖或焦磷酸的亲和力在肝脏和胰岛中相当。与遗传性或获得性糖尿病动物相比,来自对照大鼠的胰岛中UDP - 葡萄糖焦磷酸化酶的活性在患有糖尿病的动物的胰岛中略低。结合高血糖动物胰岛中糖原的积累对这些发现进行了讨论。