PURIFICATION AND PROPERTIES OF OXALIC ACID OXIDASE
PURIFICATION AND PROPERTIES OF OXALIC ACID OXIDASE
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DOI：
10.1016/0003-9861(66)90057-9
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发表时间：
1966-01-01
影响因子：
3.9
通讯作者：
CHIRIBOGA, J
中科院分区：
文献类型：
--
作者：
CHIRIBOGA, J
部分纯化大麦幼苗的可溶性酶，氧化草酸为CO2的描述。用热处理、硫酸铵分级和DEAE-纤维素层析法对大麦幼苗下胚轴和根的可溶性组分进行了纯化。该酶具有一定的底物抑制作用。该系统需要氧气，没有发现其他电子受体。该系统的Km [米氏常数]为4.2 x 10-4 [图片]。该体系由黄素和-羟基喹啉等螯合剂活化。低浓度的碘乙酸盐和氟化物（10-4 [image]）以及10-2 [image]的氰化物抑制氧化。该系统对离子强度的变化非常敏感。讨论了核黄素和S-羟基喹啉的活化机理。
The partial purification from barley seedlings of a soluble enzyme that oxidizes oxalic acid to CO2 is described. Purification of the soluble fraction of hypocotyls and roots of barley seedlings was accomplaished by heat treatment, ammonium sulfate fractionation, and DEAE-cellulose chromatography. The enzyme exhibits a definite substrate inhibitory effect. The system needs oxygen, and no other electron acceptor was found. The Km [Michaelis constant] for the system was 4.2 x 10-4 [image]. The system was activated by flavins and some chelating agents such as -hydroxyquinoline. Iodoacetate and fluoride at low concentrations (10-4 [image]) and cyanide at 10-2 [image] inhibited the oxidation. The system is very sensitive to changes in ionic strength. The mechanism of riboflavin and S hydroxyquinoline activation is discussed.