Shur S A, Skolysheva L K, Vul'fson P L
Biokhimiia. 1986 Sep;51(9):1446-53.
Phosphorylase kinase isolated from rabbit skeletal muscle contains a protein whose molecular mass as determined by polyacrylamide gel electrophoresis is 571 000 Da. The protein was found to possess a higher affinity for glycogen as compared to phosphorylase kinase and phosphorylase. The protein separated from kinase by chromatography on a DEAE-cellulose column produced during SDS electrophoresis one protein band corresponding to Mr of 95 200 Da. The above properties of the protein and the glycogen synthetase activity revealed in the presence of glucose-6-phosphate suggest that phosphorylase kinase preparations contain a hexameric form of glycogen synthetase.
从兔骨骼肌中分离出的磷酸化酶激酶含有一种蛋白质，通过聚丙烯酰胺凝胶电泳测定其分子量为571 000道尔顿。与磷酸化酶激酶和磷酸化酶相比，发现该蛋白质对糖原具有更高的亲和力。通过在DEAE-纤维素柱上进行色谱分离从激酶中分离出的该蛋白质，在SDS电泳过程中产生了一条对应于95 200道尔顿分子量的蛋白带。该蛋白质的上述特性以及在6-磷酸葡萄糖存在下显示出的糖原合成酶活性表明，磷酸化酶激酶制剂含有糖原合成酶的六聚体形式。
