Abstract
The major isozyme of alpha-glucan phosphorylase from developing maize seeds has been purified to homogeneity as verified by gel electrophoresis, ultracentrifugation and immunoprecipitation. The enzyme appears to be dimeric and has an estimated molecular weight of 223000 +/- 10000 based on ultracentrifugation, dodecylsulfate gel electrophoresis, and pyridoxal phosphate content. Adenosine diphosphoglucose appears to be a physiologically important inhibitor and interacts with the enzyme to give sigmoid kinetics when glucose 1-phosphate is the variable substrate. There are no properties of the enzyme which distinguish it from other phosphorylases as having a primarily synthetic role.
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