Tochikura T, Fukuda H, Moriguchi M
J Biochem. 1979 Jul;86(1):105-10.
The purification and properties of NADPH-linked glyoxylate reductase [EC 1. 1. 1. 79] from baker's yeast were studied. Two active fractions (peak I and peak II) were isolated by DEAE-cellulose column chromatography. The peak I fraction was purified to homogeneity by the criteria of disc gel electrophoresis and tentatively designated glyoxylate reductase I. Its molecular weight was calculated to be 31,000 from gel filtration measurements. The enzyme reduced glyoxylate 7 times faster than hydroxypyruvate and was specific for NADPH. The enzyme showed optimum activity between pH 5.5 and 7.2. The Michaelis constants for glyoxylate and NADPH were found to be 13 mM and 4 microM, respectively. The enzymic activity was not significantly affected by anions, except for nitrate and iodide, which were inhibitory.
对来自面包酵母的NADPH连接的乙醛酸还原酶[EC 1.1.1.79]的纯化及性质进行了研究。通过DEAE-纤维素柱色谱法分离出两个活性组分（峰I和峰II）。根据圆盘凝胶电泳标准，将峰I组分纯化至同质，并暂定命名为乙醛酸还原酶I。通过凝胶过滤测量计算其分子量为31,000。该酶还原乙醛酸的速度比羟基丙酮酸快7倍，且对NADPH具有特异性。该酶在pH 5.5至7.2之间表现出最佳活性。发现乙醛酸和NADPH的米氏常数分别为13 mM和4 microM。除了具有抑制作用的硝酸盐和碘化物外，阴离子对酶活性没有显著影响。
