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. 2005 Nov;25(21):9713–9723. doi: 10.1128/MCB.25.21.9713-9723.2005

FIG. 2.

FIG. 2.

Basal glycogen synthase activity in tibialis anterior (A) and gastrocnemius (B) muscle, and glycogen synthase phosphorylation level (C) and protein amount (D) in gastrocnemius muscle from WT and muscle-G4KO mice. Mice were fasted overnight. (A and B) The ratio of glycogen synthase activity represents the activity measured in the absence divided by that in the presence of glucose-6-phosphate. (C) Proteins in muscle lysates (5 μg) were separated by SDS-PAGE on 8% gels and transferred to nitrocellulose membranes. (D) Proteins in muscle lysates (50 μg) were separated by SDS-PAGE on 8% gels and transferred to nitrocellulose membranes. Glycogen synthase (GS) was visualized by immunoblotting with a glycogen synthase antibody or a phospho-specific glycogen synthase antibody. Results are means ± SEM for five to eight mice per group. OD, optical density. *, P < 0.05 versus WT.