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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Battelli M G, Lorenzoni E, Stripe F

Biochem J. 1973 Feb;131(2):191-8. doi: 10.1042/bj1310191.

The xanthine oxidase of cow's milk, crude or purified, appears as an oxidase (type O), and can be converted almost completely into a NAD(+)-dependent dehydrogenase (type D) by treatment with dithioerythritol or dihydrolipoic acid, but only to a small extent by other thiols. 2. The D form of the enzyme is inhibited by NADH, which competes with NAD(+). 3. The kinetic constants of the two forms of the enzyme are similar to those of the corresponding forms of rat liver xanthine oxidase. 4. Milk xanthine oxidase is converted into an irreversible O form by pretreatment with chymotrypsin, papain or subtilisin, but only partially with trypsin. 5. The enzyme as purified shows a major faster band and a minor slower band on gel electrophoresis. The slower band is greatly reinforced after xanthine oxidase is converted into the irreversible O form by chymotrypsin.

无论是粗制的还是纯化的牛奶黄嘌呤氧化酶，都表现为氧化酶（O型），用二硫赤藓糖醇或二氢硫辛酸处理后，几乎可以完全转化为依赖NAD(+)的脱氢酶（D型），但其他硫醇只能使其发生少量转化。2. 该酶的D型受NADH抑制，NADH与NAD(+)相互竞争。3. 两种形式的酶的动力学常数与大鼠肝脏黄嘌呤氧化酶相应形式的动力学常数相似。4. 用胰凝乳蛋白酶、木瓜蛋白酶或枯草杆菌蛋白酶预处理后，牛奶黄嘌呤氧化酶会转化为不可逆的O型，但用胰蛋白酶处理只能使其部分转化。5. 纯化后的酶在凝胶电泳上显示出一条主要的较快条带和一条次要的较慢条带。在用胰凝乳蛋白酶将黄嘌呤氧化酶转化为不可逆的O型后，较慢的条带会大大增强。

Battelli M G, Lorenzoni E, Stripe F

Biochem J. 1973 Feb;131(2):191-8. doi: 10.1042/bj1310191.

The xanthine oxidase of cow's milk, crude or purified, appears as an oxidase (type O), and can be converted almost completely into a NAD(+)-dependent dehydrogenase (type D) by treatment with dithioerythritol or dihydrolipoic acid, but only to a small extent by other thiols. 2. The D form of the enzyme is inhibited by NADH, which competes with NAD(+). 3. The kinetic constants of the two forms of the enzyme are similar to those of the corresponding forms of rat liver xanthine oxidase. 4. Milk xanthine oxidase is converted into an irreversible O form by pretreatment with chymotrypsin, papain or subtilisin, but only partially with trypsin. 5. The enzyme as purified shows a major faster band and a minor slower band on gel electrophoresis. The slower band is greatly reinforced after xanthine oxidase is converted into the irreversible O form by chymotrypsin.

无论是粗制的还是纯化的牛奶黄嘌呤氧化酶，都表现为氧化酶（O型），用二硫赤藓糖醇或二氢硫辛酸处理后，几乎可以完全转化为依赖NAD(+)的脱氢酶（D型），但其他硫醇只能使其发生少量转化。2. 该酶的D型受NADH抑制，NADH与NAD(+)相互竞争。3. 两种形式的酶的动力学常数与大鼠肝脏黄嘌呤氧化酶相应形式的动力学常数相似。4. 用胰凝乳蛋白酶、木瓜蛋白酶或枯草杆菌蛋白酶预处理后，牛奶黄嘌呤氧化酶会转化为不可逆的O型，但用胰蛋白酶处理只能使其部分转化。5. 纯化后的酶在凝胶电泳上显示出一条主要的较快条带和一条次要的较慢条带。在用胰凝乳蛋白酶将黄嘌呤氧化酶转化为不可逆的O型后，较慢的条带会大大增强。