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来自家鸡胚胎肝脏的黄嘌呤:NAD⁺氧化还原酶

Xanthine:NAD+ oxidoreductase from embryo liver of hen Gallus gallus.

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. 1990;97(1):141-3. doi: 10.1016/0305-0491(90)90192-v.

DOI:10.1016/0305-0491(90)90192-v
PMID:2253473
Abstract
  1. Xanthine:NAD+ oxidoreductase from chick embryo liver is unconvertible to the O2-dependent form, as is the enzyme from the adult hen. The Km for NAD+ (approximately 3 microM) of the embryonic enzyme is equal to, and the Km for xanthine (approximately 5 microM) is 2.5-fold lower, when compared with respective Km values of the "adult" hen enzyme. The inhibition of embryonic enzyme by NADH begins at 10 microM NADH and attains 13% at 35 microM NADH (respective data for the "adult" enzyme: 50 microM and 20% at 80 microM NADH). 2. The course of hypoxanthine----xanthine----uric acid hydroxylation catalyzed by the embryonic and "adult" enzymes is similar, however the rate of the first reaction is 2-fold lower for the embryonic enzyme. Under conditions of the limited nutritional system in the developing chick embryo, the low rate of hypoxanthine hydroxylation may promote reutilization of hypoxanthine for nucleotide synthesis.
摘要
  1. 鸡胚肝脏中的黄嘌呤:NAD⁺氧化还原酶不能转变为依赖O₂的形式,成年母鸡的该酶也是如此。与“成年”母鸡酶的相应Km值相比,胚胎酶对NAD⁺的Km(约3μM)相等,而对黄嘌呤的Km(约5μM)低2.5倍。NADH对胚胎酶的抑制作用在10μM NADH时开始,在35μM NADH时达到13%(“成年”酶的相应数据:50μM和在80μM NADH时为20%)。2. 胚胎酶和“成年”酶催化的次黄嘌呤→黄嘌呤→尿酸羟基化过程相似,然而胚胎酶催化的第一步反应速率低2倍。在发育中的鸡胚有限营养系统的条件下,次黄嘌呤羟基化的低速率可能促进次黄嘌呤再用于核苷酸合成。

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