悬浮培养的Sycamore细胞淀粉体的磷酸化酶的研究

CHARACTERIZATION OF α-1 .4-glucan PHOSPHORYLASE IN AMYLOPLASTS FROM SUSPENSION-CULTURED CELLS OF SYCAMORE (Acer pseudoplalanus L.)

用含有糖原的聚丙烯酰胺凝胶亲和电泳技术,显示悬浮培养的Syca—more(Acer pseudoplatanus L.)细胞淀粉体含有亲和力低的磷酸化酶类型(质粒类型)。蛋白质印迹法试验表明,这种磷酸化酶与马铃薯磷酸化酶的抗体发生交叉反应。这与前人报道的菠菜叶绿体和马铃薯的磷酸化酶相似,属于同一类型的磷酸化酶。

The analysis employing the affinity-polyacrylamide gel electrophoresis containing glycogen shocos that amyloplast stromal fractions of cultured cells of sycamore (Acer pseudoplalanus L.) contain a low affinity form (plastid type) phosphorylase. The immuno-blotting experiments show that amyloplast phosphorylase emerges cross reacts with the rabbit anti- sera(IgG)raised against the major phosphorylase from potato tuber. It is suggested that amyloplast phosphorylase is similar to the phosphorylase of spinach chloroplasts and potato tuber, reported by the predecessors