Fujii S, Beutler E
Acta Haematol. 1985;73(1):26-30. doi: 10.1159/000206268.
The hypothesis that human red cells contain activity of ribulose-1,5-diphosphate (Ru-1,5-P2) oxygenase, an enzyme that catalyzes the synthesis of phosphoglycolate, was examined. The putative Ru-1,5-P2 oxygenase was partially purified from human red cells using DE-52 chromatography and (NH4)2SO4 fractionation by monitoring Ru-1,5-P2-dependent 3-phosphoglycerate formation. The synthesis of [32P]phosphoglycolate from [1-32P]Ru-1,5-P2 was attempted in the presence of the partially purified preparation of the provisional Ru-1,5-P2 oxygenase. There was no formation of radioactive phosphoglycolate even under 100% oxygen gas, indicating the absence of this enzyme activity in human red cells. Together with our previous report that glycolate kinase in human red cells is not responsible for the synthesis of phosphoglycolate in vivo, these studies raise the questions whether there is actually phosphoglycolate in red cells as well as whether novel pathways for its synthesis exist.
对人类红细胞含有1,5 - 二磷酸核酮糖(Ru - 1,5 - P2)加氧酶活性这一假说进行了研究,该酶催化磷酸乙醇酸的合成。通过监测Ru - 1,5 - P2依赖性3 - 磷酸甘油酸的形成,利用DE - 52柱层析和硫酸铵分级分离从人类红细胞中部分纯化了假定的Ru - 1,5 - P2加氧酶。在部分纯化的临时Ru - 1,5 - P2加氧酶制剂存在的情况下,尝试从[1 - 32P]Ru - 1,5 - P2合成[32P]磷酸乙醇酸。即使在100%氧气条件下也没有形成放射性磷酸乙醇酸,表明人类红细胞中不存在这种酶活性。连同我们之前关于人类红细胞中的乙醇酸激酶在体内不负责磷酸乙醇酸合成的报告,这些研究提出了红细胞中是否实际存在磷酸乙醇酸以及是否存在其合成新途径的问题。