[Formation of the glycogen synthase I-glycogen complex].
A glycogen-free glycogen synthase I was isolated from rabbit skeletal muscles as a tetramer. Using the light scattering technique, the formation of the glycogen synthase I--glycogen complex was investigated; the Kd value [(0.40 +/- 0.09) X 10(-7) M], the absorption capacity of glycogen towards the enzyme [aM = (1.89 +/- 0.4) X 10(-6) mol] and the number of enzyme-binding sites per polysaccharide molecule (n = 10) were determined, using rabbit liver glycogen (Mr = 5.28 X 10(6)). After the formation of the glycogen synthase I--glycogen complex has been completed, the reactivity of some SH-groups of the enzyme is reduced and some of them become masked towards 5,5'-dithiobis-2-nitrobenzoate.
D000327:Adsorption; D000818:Animals; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D006006:Glycogen Synthase / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D008112:Liver Glycogen / Q000378:metabolism*; D008623:Mercaptoethanol / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D013438:Sulfhydryl Compounds / Q000378:metabolism; D000516:alpha-Amylases / Q000378:metabolism
D008112:Liver Glycogen; D013438:Sulfhydryl Compounds; D008623:Mercaptoethanol; D006006:Glycogen Synthase; D000516:alpha-Amylases
Izuchenie obrazovaniia kompleksa glikogensintazy I s glikogenom.