Botanisches Institut der Universität, Schloßgarten 3, D-4400, Münster, Federal Republic of Germany.
Planta. 1979 Jan;145(1):69-75. doi: 10.1007/BF00379929.
Starch phosphorylase activity in extracts of spinach or pea leaves and of isolated chloroplasts was determined and separated by electrophoresis in polyacrylamide gels. In spinach leaf extracts, a specific activity of 16 nmol glucose 1-phosphate formed per min per mg protein was found, whereas a lower value (6 nmol per min per mg protein) was observed in preparations of isolated chloroplasts which were about 75% intact. In the spinach leaf extracts two forms of phosphorylase were found; chloroplast preparations almost exclusively contained one of these. In pea leaf extracts the specific activity was 10 nmol glucose 1-phosphate formed per min per mg protein. Three forms of phosphorylase contributed to this activity. Preparations of isolated chloroplasts with an intactness of about 85% exhibited a lower specific activity (5nmol per min per mg protein) and contained two of these three phosphorylase forms.
用聚丙酰胺凝胶电泳法对菠菜或豌豆叶片提取物及分离的叶绿体中的淀粉磷酸化酶活性进行了测定和分离。在菠菜叶片提取物中，每毫克蛋白每分钟可形成 16 毫摩尔葡萄糖-1-磷酸，而分离的叶绿体制剂中（大约 75%完整）每毫克蛋白每分钟可形成 6 毫摩尔葡萄糖-1-磷酸，其活性较低。在菠菜叶片提取物中发现了两种形式的磷酸化酶；叶绿体制剂几乎只含有其中的一种。在豌豆叶片提取物中，每毫克蛋白每分钟可形成 10 毫摩尔葡萄糖-1-磷酸。三种形式的磷酸化酶对这种活性都有贡献。完整度约为 85%的分离叶绿体制剂表现出较低的比活性（5 毫摩尔每分钟每毫克蛋白），并含有这三种磷酸化酶形式中的两种。
