Fry D W, Richardson K E
Biochim Biophys Acta. 1979 May 10;568(1):135-44. doi: 10.1016/0005-2744(79)90281-x.
Glycolic acid oxidase has been isolated from human liver and purified over 3000-fold to a specific activity of 123 U/mg protein by a 5-step procedure. The preparation gave a single protein band on polyacrylamide gel electrophoresis, required flavin mononucleotide for catalytic activity, had a pH optimum between 8.2-8.8 depending on the substrate, and had a molecular weight of 105 000. The enzyme has a broad specificity towards alpha-hydroxy acids. Glycolate (Km = 3.3 . 10(-4) M) was the most effective substrate. The enzyme was stable for several months when stored as an (NH4)2SO4 precipitate or in 15% glycerol. Since glycolate inhibits the oxidation of glyoxylate to oxalate by glycolic acid oxidase, it is suggested that glycolic acid oxidase contributes to the synthesis of oxalate in vivo when the glyoxylate concentration is high and the glycolate concentration is low.
乙醇酸氧化酶已从人肝脏中分离出来，并通过五步程序纯化了3000多倍，比活性达到123 U/mg蛋白质。该制剂在聚丙烯酰胺凝胶电泳上呈现单一蛋白条带，催化活性需要黄素单核苷酸，根据底物不同，最适pH在8.2 - 8.8之间，分子量为105000。该酶对α - 羟基酸具有广泛的特异性。乙醇酸（Km = 3.3×10⁻⁴ M）是最有效的底物。当以硫酸铵沉淀形式或保存在15%甘油中时，该酶可稳定保存数月。由于乙醇酸可抑制乙醇酸氧化酶将乙醛酸氧化为草酸盐，因此有人提出，当乙醛酸浓度高而乙醇酸浓度低时，乙醇酸氧化酶在体内草酸盐的合成中起作用。
