[Characteristic properties of the complex of glycogen synthase with glycogen].
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.
D000818:Animals; D006003:Glycogen / Q000302:isolation & purification / Q000378:metabolism*; D006006:Glycogen Synthase / Q000302:isolation & purification / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D011485:Protein Binding; D011817:Rabbits
D006003:Glycogen; D006006:Glycogen Synthase
Kharakteristika svoĭstv kompleksa glikogensintazy I s glikogenom.