Two forms of α-glucan phosphorylase were isolated fromDioscorea cayenensis by ammonium sulphate gradient solubilization and further purified using starch adsorption and ion exchange chromatography on DEAE-Sephadex A-25 colunm. Fraction DC1was purified 80 fold with specific activity of 400 umol min−1 mg−1 protein, while fraction DC2showed 60 fold purification with specific activity of 300 umol min−1 mg−1 protein. Both enzyme forms were activated by AMP, magnesium, calcium and inhibited by ATP, ADP, ADP-glucose and sodium sulphate. They showed absolute primer requirement and obeyed Michaelis-Menten kinetics. The two forms have different Km values and different pH optima. The presence of amino acids and intermediates of glycolysis had no effect on the activities of the enzymes. There are no unusual properties of the enzymes which suggest that they function primarily in starch biosynthesis inD. cayenensis tuber.