When at liver homogenates were incubated with 1mM $CCl_4$ for five min, glycogen level was decreased, while treatment with protein fraction $G_4$ increased the glycogen level. In addition $G_4$ inhibited the phosphorylation of 34 KD and 118 KD polypeptides induced by $CCl_4$. These protein were more strongly phosphorylated by $Ca^{2+}$/calmodulin-dependent kinase than by C-kinase. Since 34 KD polypeptide was solely phosphorylated by NaF (50mM), an inhibitor of both glycogen syntheses and phosphoprotein phosphates, it is inferred that 3 KD polypeptide is glycogen synthase-likd protein. Because glycogen synthesis is inhibited by phosphorylation of $Ca^{2+}$-dependent glycogen syntheses, it is suggested that $G_4$ increased liver glycogen level by inhibiting phosphorylation of 34 KD polypeptide which is thought to glycogen syntheses-like protein.