1978 95-106(Eingegangen am 22.12.1976) Cell extracts of Cryptococcue laurentii, a yeast which synthesizes amylose when grown a t low pH, contained an a-glucan phosphorylase (a-1 -4)-glucan: orthophosphate glucosyl transferase (EC 2.4.1.1). The enzyme, which is very labile, showed greatest stability a t pH 8.0 in the presence of 0.1 M @-glycerophosphate and 0.1 M sodium fluoride. Based upon visible colour development with iodine a cell homogenate, centrifuged a t 32,000 g to remove cell debris, synthesized starch-like polymers upon incubation with glucose-1-phosphate in a p H range of 5.6-6.1. Based upon incorporation of labelled glucose from glucose-1-phosphate the pH of maximum activity was 5.9-6.2. The enzyme was partially purified by glycogen complexing, precipitation, and adsorption on hydroxylapatite followed by elution. The purified enzyme has a K, for glucose-lphosphate of 1.6 x lo-' M. Mutants impaired in their ability to synthesize amylose contained approximately one fourth of the phosphorylase activity as compared to the wild type. The possible role of the glucan phosphorylase in amylose biosynthesis is discussed.