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1
ACCELERATING EFFECT OF COPPER ION ON THE REACTIVATION OF REDUCED TAKA-AMYLASE A THROUGH CATALYSIS OF THE OXIDATION OF SULFHYDRYL GROUPS.铜离子通过催化巯基氧化对还原型高峰淀粉酶A再活化的加速作用
J Biochem. 1964 Oct;56:344-50. doi: 10.1093/oxfordjournals.jbchem.a127999.
2
INACTIVATION OF MYOSIN BY 2,4-DINITROPHENOL AND PROTECTION BY ADENOSINE TRIPHOSPHATE AND OTHER PHOSPHATE COMPOUNDS.2,4-二硝基苯酚对肌球蛋白的失活作用以及三磷酸腺苷和其他磷酸盐化合物的保护作用
J Biol Chem. 1963 Nov;238:3654-9.
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Relation between modification of functional groups of proteins and their biological activity. I.A graphical method for the determination of the number and type of essential groups.蛋白质官能团修饰与其生物活性之间的关系。I. 一种确定必需基团数量和类型的图解方法。
Sci Sin. 1962 Nov;11:1535-58.
4
Effect of NADH on hypoxanthine hydroxylation by native NAD+-dependent xanthine oxidoreductase of rat liver, and the possible biological role of this effect.NADH对大鼠肝脏天然NAD⁺依赖性黄嘌呤氧化还原酶催化的次黄嘌呤羟基化作用的影响及其该作用可能的生物学意义。
Biochem J. 1981 Dec 15;200(3):597-603. doi: 10.1042/bj2000597.
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Mechanisms of inactivation of molybdoenzymes by cyanide.氰化物使钼酶失活的机制。
J Biol Chem. 1980 Apr 10;255(7):2694-9.
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A sensitive radioassay for sulfhydryl groups with tetraethylthiuram disulfide.一种用二硫化四乙基秋兰姆进行巯基检测的灵敏放射分析方法。
J Biol Chem. 1966 Jul 10;241(13):3036-40.
7
Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties.乳黄嘌呤氧化酶D型（脱氢酶）和O型（氧化酶）。纯化、相互转化及某些性质
Biochem J. 1973 Feb;131(2):191-8. doi: 10.1042/bj1310191.
8
The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme.大鼠肝脏黄嘌呤氧化酶的调节。巯基在酶活性从脱氢酶（D型）转化为氧化酶（O型）过程中的作用及酶的纯化。
Biochem J. 1972 Feb;126(3):739-45. doi: 10.1042/bj1260739.
9
The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O).大鼠肝脏黄嘌呤氧化酶的调节。该酶活性在体外从脱氢酶（D型）向氧化酶（O型）的转化。
J Biol Chem. 1969 Jul 25;244(14):3855-63.
10
The copper catalyzed oxidation of cysteine to cystine.铜催化的半胱氨酸氧化为胱氨酸的反应。
Arch Biochem Biophys. 1969 Mar;130(1):354-61. doi: 10.1016/0003-9861(69)90044-7.

单个巯基参与大鼠肝脏黄嘌呤氧化还原酶从依赖NAD⁺的活性向依赖O₂的活性的转变过程。

Involvement of a single thiol group in the conversion of the NAD+-dependent activity of rat liver xanthine oxidoreductase to the O2-dependent activity.

作者信息

Kamiński Z W, Jezewska M M

出版信息

Biochem J. 1982 Nov 1;207(2):341-6. doi: 10.1042/bj2070341.

DOI:10.1042/bj2070341
PMID:6961918
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1153866/
Abstract

The effects of 2-iodosobenzoic acid, 4-chloromercuribenzoate, 5,5'-dithiobis-(2-nitrobenzoic acid) and tetraethylthioperoxydicarbonic diamide (disulphiram) on the NAD+-dependent activity of xanthine oxidoreductase from rat liver were investigated. Only disulphiram converted the NAD+-dependent activity into the O2-dependent activity quantitatively, without changing the xanthine hydroxylation rate. The modification process was a first-order reaction with respect to time (min) and disulphiram concentration (microM). The kinetic data showed that modification of single thiol group is sufficient for loss of the enzymic activity towards NAD+ as electron acceptor. The complete protection afforded by NAD+ against the action of disulphiram suggests that the essential thiol group may be involved in binding of NAD+ to the xanthine oxidoreductase molecule.

摘要

研究了2-碘代苯甲酸、4-氯汞苯甲酸、5,5'-二硫代双-(2-硝基苯甲酸)和四乙基硫代过氧二碳酸二酰胺（双硫仑）对大鼠肝脏黄嘌呤氧化还原酶NAD⁺依赖性活性的影响。只有双硫仑能将NAD⁺依赖性活性定量地转化为O₂依赖性活性，而不改变黄嘌呤羟化速率。修饰过程是关于时间（分钟）和双硫仑浓度（微摩尔）的一级反应。动力学数据表明，单个巯基的修饰足以使酶对作为电子受体的NAD⁺失去活性。NAD⁺对双硫仑作用的完全保护表明，必需的巯基可能参与NAD⁺与黄嘌呤氧化还原酶分子的结合。