Kholmina G V, Gorkin V Z
Vopr Med Khim. 1979 May-Jun;25(3):322-8.
A protein fraction, which did not contain NADP [or NADPH]-dependent aldehyde reductase as well as NAD [or NADP]-dependent aldehyde dehydrogenases, but which catalyzed oxidation of fatty-aromatic aldehydes, was isolated from extract of rat liver tissue using ammonium sulfate fractionation combined with gradient syvorptive chromatography on DEAE-Sephadex A-25 [or Molselect DEAE-25], CM-Sephadex C-25 and gel-filtration on Sephadex G-200. Investigations of molecular weight and catalytic properties of the protein fraction obtained enabled to identify it with xanthine oxidase [EC 1.2.3.2]. Aldehyde dehydrogenases as well as xanthine oxidase are involved in oxidation of fatty-aromatic aldehydes to corresponding fatty acids, besides the reduction of the aldehydes to alcohols, catalyzed by aldehyde reductase and alcohol dehydrogenases.
从大鼠肝脏组织提取物中,通过硫酸铵分级分离,结合在DEAE - Sephadex A - 25(或Molselect DEAE - 25)、CM - Sephadex C - 25上的梯度吸附色谱以及在Sephadex G - 200上的凝胶过滤,分离出一种蛋白质组分。该组分不含依赖NADP[或NADPH]的醛还原酶以及依赖NAD[或NADP]的醛脱氢酶,但能催化脂肪族 - 芳香族醛的氧化。对所得蛋白质组分的分子量和催化特性进行研究后,确定其为黄嘌呤氧化酶[EC 1.2.3.2]。醛脱氢酶以及黄嘌呤氧化酶都参与脂肪族 - 芳香族醛氧化为相应脂肪酸的过程,此外,醛还原酶和醇脱氢酶可催化醛还原为醇。