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Title: [Characteristic properties of the complex of glycogen synthase with glycogen]. Author: Solov'eva GA, Sakharova IS, Krivokobyl'skaia IaI. Journal: Biokhimiia; 1982 Sep; 47(9):1563-9. PubMed ID: 6814538. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]