Meggio F, Flamigni F, Guarnieri C, Pinna L A
Biochim Biophys Acta. 1987 Jun 15;929(1):114-6. doi: 10.1016/0167-4889(87)90246-1.
The sizes of the radiolabeled fragments obtained by CNBr and DMSO/HBr digestion of 32P-labeled ornithine decarboxylase phosphorylated by rat liver casein kinase TS (type-2) are consistent with the location of the phosphorylation site within the sequence(303-309) Ser-Asp-Asp-Glu-Asp-Glu-Ser. Parallel experiments with synthetic peptides rule out the suitability of Ser-309, as well as of other serines of ornithine decarboxylase having just two or three acidic residues close to their C terminal side. Ser-303 appears, therefore, to be the main if not the only target for casein kinase-2.
用大鼠肝酪蛋白激酶TS（2型）磷酸化的32P标记的鸟氨酸脱羧酶经CNBr和DMSO/HBr消化后得到的放射性标记片段的大小，与序列（303 - 309）Ser - Asp - Asp - Glu - Asp - Glu - Ser内磷酸化位点的位置一致。用合成肽进行的平行实验排除了Ser - 309以及鸟氨酸脱羧酶其他丝氨酸（其C末端侧仅有两个或三个酸性残基）作为磷酸化位点的可能性。因此，Ser - 303似乎是酪蛋白激酶2的主要（如果不是唯一的）作用靶点。
