绿蟾蜍（Bufo viridis）及其他脊椎动物肝脏中黄嘌呤：NAD⁺氧化还原酶的比较
Comparison of xanthine: NAD+ oxidoreductase from liver of toad Bufo viridis and other vertebrates.
作者信息
Zakrzewska B, Jezewska M M
机构信息
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
出版信息
Comp Biochem Physiol B. 1989;94(2):361-5. doi: 10.1016/0305-0491(89)90356-8.
PMID:2591196
Abstract
- Xanthine oxidoreductase was isolated from toad Bufo viridis (a mainly ureotelic amphibian species) and partially purified. The enzyme occurred as a stable xanthine: NAD+ oxidoreductase (EC 1.1.1.204), unconvertible to the oxidase form. 2. Some properties of the enzyme resembled those of xanthine oxidoreductase from an ammonotelic fish, Cyprinus carpio, and the ureotelic rat, but in other aspects it was similar to this enzyme from an uricotelic snake, Natrix natrix. 3. Inhibition of the toad enzyme by NADH at high non-physiological concentrations rules out a modulation of its oxypurine-hydroxylating activity by in vivo changes in the NADH/NAD+ ratio. Therefore, toad xanthine oxidoreductase plays no regulatory role in the purine nucleotide metabolism.
摘要
- 从绿蟾蜍（一种主要排尿素的两栖动物）中分离出黄嘌呤氧化还原酶并进行部分纯化。该酶以稳定的黄嘌呤：NAD⁺氧化还原酶（EC 1.1.1.204）形式存在，无法转化为氧化酶形式。2. 该酶的一些特性类似于来自排氨鱼类鲤鱼和排尿素大鼠的黄嘌呤氧化还原酶，但在其他方面，它与来自排尿酸蛇草游蛇的这种酶相似。3. 在高非生理浓度下，NADH对蟾蜍酶的抑制排除了通过体内NADH/NAD⁺比值变化对其氧化嘌呤羟化活性进行调节的可能性。因此，蟾蜍黄嘌呤氧化还原酶在嘌呤核苷酸代谢中不发挥调节作用。
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