Potato glycogen phosphorylase (EC2.4.1.1) was purified through extraction from potato starch grains using β-cyclodextrin followed by the preparative affinity erectrophoresis on a slab type apparatus. From 10 kg of potato tubers 2.1 mg of the homogeneous phosphorylase was obtained at a yield of 45%. Its molecular weight was estimated as 18×10^4 from the gel filtration. The enzyme was composed of two identical subunits of molecular weight of 9×10^4. The amino acid composition was distantly related to the potato starch phosphorylase. While the starch phosphorylase has practically no affinity with α-(1,4)-D-gucan, the glycogen phosphorylase has a that the affinity difference between these phosphorylases is due to a difference in their glycogen storage sites.