Ciudad C, DePaoli-Roach A, Roach P J
Biochim Biophys Acta. 1984 Jun 19;804(2):261-3. doi: 10.1016/0167-4889(84)90158-7.
Specific antibodies were used to purify glycogen synthase from isolated rabbit hepatocytes that had been incubated in a medium containing [32P]phosphate. The enzyme gave rise to two main 32P-labeled CNBr fragments of electrophoretic mobilities similar to those obtained after phosphorylation of the enzyme by individual protein kinases in vitro.
使用特异性抗体从在含有[32P]磷酸盐的培养基中孵育过的离体兔肝细胞中纯化糖原合酶。该酶产生了两个主要的32P标记的溴化氰片段，其电泳迁移率类似于该酶在体外被单个蛋白激酶磷酸化后获得的电泳迁移率。
