Brownsey R W, Hughes W A, Denton R M
Biochem J. 1977 Dec 15;168(3):441-5. doi: 10.1042/bj1680441.
Intact rat epididymal fat-cells were incubated with 32Pi and the intracellular proteins separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. One of the phosphorylated proteins has the same RF value as [14C]biotin-labelled acetyl-CoA carboxylase purified from fat-cells and is specifically precipitated after incubation with antiserum raised against acetyl-CoA carboxylase. No significant changes in the extent of phosphorylation of acetyl-CoA carboxylase were detected after exposure of the cells to insulin.
将完整的大鼠附睾脂肪细胞与32Pi一起孵育,然后通过十二烷基硫酸钠/聚丙烯酰胺凝胶电泳分离细胞内蛋白质。其中一种磷酸化蛋白的Rf值与从脂肪细胞中纯化的[14C]生物素标记的乙酰辅酶A羧化酶相同,并且在用抗乙酰辅酶A羧化酶产生的抗血清孵育后会被特异性沉淀。在细胞暴露于胰岛素后,未检测到乙酰辅酶A羧化酶磷酸化程度的显著变化。