Meggio F, Flamigni F, Caldarera C M, Guarnieri C, Pinna L A
Biochem Biophys Res Commun. 1984 Aug 16;122(3):997-1004. doi: 10.1016/0006-291x(84)91190-2.
Highly purified preparations of rat heart ornithine decarboxylase are readily phosphorylated by rat liver type-2 casein kinase-TS at the same 54 KDa protein band which is also radiolabeled by 3H-DFMO. The reaction, which is stimulated by polylysine leads to the incorporation of up to 0.8 mol P/mol ornithine decarboxylase at seryl residue(s) included in a single 8.6 KDa CNBr fragment. Partially purified preparations of ornithine decarboxylase contain a type-2 casein kinase which promotes the phosphorylation of ornithine decarboxylase at the same CNBr fragment affected by rat liver casein kinase-TS.
大鼠心脏鸟氨酸脱羧酶的高度纯化制剂很容易被大鼠肝脏2型酪蛋白激酶-TS在相同的54 kDa蛋白条带上磷酸化,该条带也被3H-DFMO放射性标记。该反应受聚赖氨酸刺激,导致在单个8.6 kDa CNBr片段中的丝氨酸残基处,每摩尔鸟氨酸脱羧酶掺入多达0.8摩尔磷。鸟氨酸脱羧酶的部分纯化制剂含有一种2型酪蛋白激酶,它能促进鸟氨酸脱羧酶在受大鼠肝脏酪蛋白激酶-TS影响的相同CNBr片段上的磷酸化。