Purification of bovine heart glycogen synthase.
Glycogen synthase was purified to apparent homogeneity from bovine heart muscle by a procedure involving precipitation of the enzyme in the presence of added glycogen by polyethylene glycol, chromatography on DEAE-Sephacel, and high-speed centrifugation through a sucrose-containing buffer. The enzyme was maintained in the presence of glycogen during the isolation procedure. Glycogen synthase I and D preparations were obtained having specific activities of 21-25 and 30-35 units/mg protein at pH 7.8 and 30 degrees C and having activity ratios of 0.5-0.6 and 0.05-0.10, respectively, when assayed in the absence and in the presence of glucose 6-P.
D000818:Animals; D002417:Cattle; D002498:Centrifugation; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D004589:Electrophoresis, Disc; D006006:Glycogen Synthase / Q000302:isolation & purification*; D009206:Myocardium / Q000201:enzymology*
D006006:Glycogen Synthase