Risø National Laboratory, Agricultural Research Department, DK-4000, Roskilde, Denmark.
Planta. 1980 Apr;148(4):412-6. doi: 10.1007/BF00388131.
The activity of soluble starch synthetase (ADP-glucose: α-1,4-glucan α-4-glucosyltransferase) in the non-purified extract from 16 day-old Bomi barley endosperms (Hordeum vulgare L.) was low and the reaction was non-linear when plotted against protein concentration. Starch synthetase was purified by ammonium sulfate precipitation and DEAE-cellulose chromatography and separated into four fractions. In the absence of an added carbohydrate primer two of the four fractions catalized the synthesis of a methanol-precipitable α-glucan when high concentrations of sodium citrate and bovine serum albumim were added. The rate of α-glucan synthesis by the unprimed reaction was higher than for the primed reaction. The four enzyme fractions were active with ADP-Glc, but not with UDP-Glc, both in the primed and in the unprimed reaction.
16 日龄波密青稞胚乳（Hordeum vulgare L.）非纯化提取物中可溶性淀粉合酶（ADP-葡萄糖：α-1,4-葡聚糖α-4-葡萄糖基转移酶）的活性较低，当与蛋白质浓度作图时，反应呈非线性。淀粉合酶通过硫酸铵沉淀和 DEAE-纤维素层析进行纯化，并分离成四个部分。在没有添加碳水化合物引物的情况下，当添加高浓度的柠檬酸钠和牛血清白蛋白时，四个部分中的两个可以催化甲醇沉淀的α-葡聚糖的合成。无引物反应的α-葡聚糖合成速率高于引物反应。四个酶部分均能与 ADP-Glc 反应，而不能与 UDP-Glc 反应，无论是在引物反应还是无引物反应中。
