An algal α-glucan phosphorylase which requires adenosine-5-phosphate as coenzyme

Abstract

Previous homogeneous preparations of algal α-1,4-glucan: orthophosphate glucosyl transferase (phosphorylase), when subjected to disc electrophoresis on polyacrylamide gel proved to contain at least two fractions which had the ability to synthesize linear glucans from glucosyl phosphate. By the use of a modified Gomori technique, where the phosphate liberated by the enzyme from glucosyl phosphate is precipitated in situ as the insoluble calcium salt, converted to the silver salt by treatment with silver nitrate, and this then reduced to black metallic silver by ultra-violet irradiation, it has been possible to further delineate these two phosphorylases. The significance of this situation is explored with a view to the possible similarities existing in these enzymes between plants and animals.