Solov'eva G A, Sakharova I S, Krivokobyl'skaia Ia I
Biokhimiia. 1982 Sep;47(9):1563-9.
The glycogen synthase I--glycogen complex isolated from rabbit skeletal muscles is stable during precipitation with trichloroacetic acid and Sepharose 2B chromatography. The complex catalyzes the synthesis (lengthening) of the alpha-1.4-glucosyl chains when endogenous or exogenous enzyme-free glycogen is used, the initial rates of this synthesis being identical. Preincubation with glycogen does not cause activation of the complex or formation of additional glycogen synthase I--polysaccharide bonds. The complex is characterized by saturation with respect to glycogen; the molar concentration ratios of the non-reducible chain and protein monomer within the complex does not exceed 100. An increase in the length of the synthesized alpha-1.4-glycosyl chains of glycogen results in a decrease of the rate of the glycogen synthase reaction in time.
从兔骨骼肌中分离出的糖原合酶I-糖原复合物，在三氯乙酸沉淀和琼脂糖2B层析过程中是稳定的。当使用内源性或外源性无酶糖原时，该复合物催化α-1,4-葡糖基链的合成（延长），这种合成的初始速率是相同的。与糖原预孵育不会导致复合物的激活或额外的糖原合酶I-多糖键的形成。该复合物的特征是对糖原饱和；复合物中非还原链与蛋白质单体的摩尔浓度比不超过100。糖原合成的α-1,4-糖基链长度增加会导致糖原合酶反应速率随时间降低。
