Salsas E, Larner J
J Biol Chem. 1975 Mar 10;250(5):1833-7.
Glycogen synthase purified to homogeneity from rabbit skeletal muscle is essentially free of carbohydrate and shows no activity in the absence of added acceptor. It can use glucose as a substrate converting it to a glucose disaccharide in the presence of UDP-glucose as cosubstrate. The reaction is dependent on time, and on UDP-glucose, glucose, and enzyme concentrations. The product of the single step reaction co-chromatographs in two solvent systems with maltose. The glucose disaccharide produced in the reaction with UDP-[14-C]glucose and nonradioactive glucose as well as with nonradioactive UDP-glucoes and [14-C]glucose is labeled asymmetrically. The linkage is characterized as alpha-1,4 and therefore the disaccharide is identified as maltose.
从兔骨骼肌中纯化至同质的糖原合酶基本不含碳水化合物,且在没有添加受体的情况下无活性。它可以利用葡萄糖作为底物,在以UDP-葡萄糖作为共底物存在时将其转化为葡萄糖二糖。该反应依赖于时间、UDP-葡萄糖、葡萄糖和酶的浓度。单步反应的产物在两种溶剂系统中与麦芽糖共色谱。与UDP-[14-C]葡萄糖和非放射性葡萄糖以及与非放射性UDP-葡萄糖和[14-C]葡萄糖反应产生的葡萄糖二糖被不对称标记。该连接被表征为α-1,4,因此该二糖被鉴定为麦芽糖。