Ariño J, Mor A, Bosch F, Baanante I V, Guinovart J J
FEBS Lett. 1984 May 21;170(2):310-4. doi: 10.1016/0014-5793(84)81334-4.
The effects of epinephrine and vasopressin on the phosphorylation state of glycogen synthase were studied using rat hepatocytes incubated with 32P. After the incubation with hormones, 32P-labeled glycogen synthase was isolated using antibodies against rat liver enzyme. The immunoprecipitate showed a single radioactive band ( Mapp 88 kDa) when subjected to SDS-gel electrophoresis. Both epinephrine and vasopressin inactivated the enzyme and increased the 32P content of glycogen synthase. Cleavage of the immunoprecipitate with CNBr yielded two major 32P-labeled fragments of Mapp approximately 27 and 12 kDa. Both hormones increased the 32P content of both fragments. These results prove that epinephrine and vasopressin increase the phosphate content of the enzyme promoting its phosphorylation at multiple sites.
利用用³²P孵育的大鼠肝细胞研究了肾上腺素和血管加压素对糖原合酶磷酸化状态的影响。在用激素孵育后，使用针对大鼠肝脏酶的抗体分离出³²P标记的糖原合酶。免疫沉淀物在进行SDS-凝胶电泳时显示出一条单一的放射性条带（表观分子量88 kDa）。肾上腺素和血管加压素均使该酶失活，并增加了糖原合酶的³²P含量。用溴化氰切割免疫沉淀物产生了两个主要的³²P标记片段，表观分子量约为27 kDa和12 kDa。两种激素均增加了两个片段的³²P含量。这些结果证明，肾上腺素和血管加压素增加了该酶的磷酸含量，促进其在多个位点的磷酸化。
