Guitton C, Mache R
Eur J Biochem. 1987 Jul 1;166(1):249-54. doi: 10.1111/j.1432-1033.1987.tb13509.x.
A protein kinase activity responsible for the in vitro phosphorylation of at least six endogenous polypeptides including the large subunit of the ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) is present in the stroma (3000 X g supernatant, S30) of spinach chloroplasts. The phosphorylation of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit is strongly enhanced when sodium fluorure is used as a protein phosphatase inhibitor. Phosphorylation occurs on threonine and serine residues. The protein kinase involved is not Ca2+-dependent. There is also evidence for a protein phosphatase activity which suggests a coupled regulation by a phosphorylation-dephosphorylation process. The phosphorylating activity is drastically reduced when S30 is prepared from leaves harvested after a dark period. Phosphorylation of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit is not related to its own synthesis. The in vitro phosphorylation of the glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) is also demonstrated.
菠菜叶绿体基质（3000×g上清液，S30）中存在一种蛋白激酶活性，它负责体外磷酸化至少六种内源性多肽，包括核酮糖-1,5-二磷酸羧化酶/加氧酶（EC 4.1.1.39）的大亚基。当使用氟化钠作为蛋白磷酸酶抑制剂时，核酮糖-1,5-二磷酸羧化酶/加氧酶大亚基的磷酸化会显著增强。磷酸化发生在苏氨酸和丝氨酸残基上。所涉及的蛋白激酶不依赖Ca2+。也有证据表明存在蛋白磷酸酶活性，这表明通过磷酸化-去磷酸化过程进行耦合调节。当从黑暗期后收获的叶片制备S30时，磷酸化活性会急剧降低。核酮糖-1,5-二磷酸羧化酶/加氧酶大亚基的磷酸化与其自身合成无关。还证明了3-磷酸甘油醛脱氢酶（EC 1.2.1.13）的体外磷酸化。
