• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利：CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法，用中文像聊天一样搜索，搜遍4000万医学文献。AI智能推荐，让科研检索更轻松。

立即免费搜索

文件翻译

保留排版，准确专业，支持PDF/Word/PPT等文件格式，支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述，25分钟生成高质量综述，智能提取关键信息，辅助科研写作。

立即免费体验

2,2'-二硫代二吡啶激活醛脱氢酶，并保护该酶免受双硫仑的失活作用。

2,2'-Dithiodipyridine activates aldehyde dehydrogenase and protects the enzyme against inactivation by disulfiram.

作者信息

Kitson T M

出版信息

Biochem J. 1979 Dec 1;183(3):751-3. doi: 10.1042/bj1830751.

DOI:10.1042/bj1830751
PMID:540042
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1161658/
Abstract

Small concentrations of 2,2'-dithiodipyridine cause a rapid activation of sheep liver cytoplasmic aldehyde dehydrogenase in the presence of NAD+. Enzyme pre-modified by 2,2'-dithiodipyridine is largely protected against the potent inactivatory effect of disulfiram. 2,2'-Dithiobis-(5-nitropyridine) inactivates the enzyme. The implications of these results are discussed with reference to various possible classes of thiol group in aldehyde dehydrogenase.

摘要

在烟酰胺腺嘌呤二核苷酸（NAD⁺）存在的情况下，低浓度的2,2'-二硫代二吡啶会使绵羊肝脏细胞质醛脱氢酶迅速活化。经2,2'-二硫代二吡啶预先修饰的酶在很大程度上可免受双硫仑的强效失活作用影响。2,2'-二硫代双（5-硝基吡啶）会使该酶失活。本文参照醛脱氢酶中各种可能的巯基类别对这些结果的意义进行了讨论。

相似文献

1
2,2'-Dithiodipyridine activates aldehyde dehydrogenase and protects the enzyme against inactivation by disulfiram.2,2'-二硫代二吡啶激活醛脱氢酶，并保护该酶免受双硫仑的失活作用。
Biochem J. 1979 Dec 1;183(3):751-3. doi: 10.1042/bj1830751.
2
Further studies of the action of disulfiram and 2,2'-dithiodipyridine on the dehydrogenase and esterase activities of sheep liver cytoplasmic aldehyde dehydrogenase.双硫仑和2,2'-二硫代二吡啶对绵羊肝脏细胞质醛脱氢酶的脱氢酶和酯酶活性作用的进一步研究
Biochem J. 1982 Jun 1;203(3):743-54. doi: 10.1042/bj2030743.
3
The time course of the interaction of sheep liver cytoplasmic aldehyde dehydrogenase with 2,2'- and 4,4'-dithiodipyridine: a comparison with the action of disulfiram.
Arch Biochem Biophys. 1984 Nov 1;234(2):487-96. doi: 10.1016/0003-9861(84)90296-0.
4
High concentrations of aldehydes slow the reaction of cytoplasmic aldehyde dehydrogenase with thiol-group modifiers.高浓度的醛类物质会减缓细胞质醛脱氢酶与硫醇基团修饰剂的反应。
Biochem J. 1985 Jun 15;228(3):765-7. doi: 10.1042/bj2280765.
5
The activation of aldehyde dehydrogenase by diethylstilboestrol and 2,2'-dithiodipyridine.己烯雌酚和2,2'-二硫代二吡啶对醛脱氢酶的激活作用。
Biochem J. 1982 Oct 1;207(1):81-9. doi: 10.1042/bj2070081.
6
Modification of thiol groups in cytoplasmic aldehyde dehydrogenase.
Alcohol. 1985 Jan-Feb;2(1):97-101. doi: 10.1016/0741-8329(85)90023-0.
7
Reaction between sheep liver mitochondrial aldehyde dehydrogenase and various thiol-modifying reagents.绵羊肝脏线粒体醛脱氢酶与各种硫醇修饰试剂之间的反应。
Biochem J. 1989 Jul 1;261(1):281-4. doi: 10.1042/bj2610281.
8
Effects of diethylstilbestrol, 2,2'-dithiodipyridine, and chloral hydrate on the esterase activity of sheep liver cytoplasmic aldehyde dehydrogenase.己烯雌酚、2,2'-二硫代二吡啶和水合氯醛对绵羊肝脏细胞质醛脱氢酶酯酶活性的影响。
Biochemistry. 1986 Aug 12;25(16):4718-24. doi: 10.1021/bi00364a040.
9
The effect of 5,5'-dithiobis(1-methyltetrazole) on cytoplasmic aldehyde dehydrogenase and its implications for cephalosporin-alcohol reactions.
Alcohol Clin Exp Res. 1986 Jan-Feb;10(1):27-32. doi: 10.1111/j.1530-0277.1986.tb05608.x.
10
The inactivation of aldehyde dehydrogenase by disulfiram in the presence of glutathione.在谷胱甘肽存在的情况下，双硫仑使乙醛脱氢酶失活。
Biochem J. 1981 Oct 1;199(1):255-8. doi: 10.1042/bj1990255.

引用本文的文献

1
The inactivation of aldehyde dehydrogenase by disulfiram in the presence of glutathione.在谷胱甘肽存在的情况下，双硫仑使乙醛脱氢酶失活。
Biochem J. 1981 Oct 1;199(1):255-8. doi: 10.1042/bj1990255.
2
The activation of aldehyde dehydrogenase by diethylstilboestrol and 2,2'-dithiodipyridine.己烯雌酚和2,2'-二硫代二吡啶对醛脱氢酶的激活作用。
Biochem J. 1982 Oct 1;207(1):81-9. doi: 10.1042/bj2070081.
3
Further studies of the action of disulfiram and 2,2'-dithiodipyridine on the dehydrogenase and esterase activities of sheep liver cytoplasmic aldehyde dehydrogenase.双硫仑和2,2'-二硫代二吡啶对绵羊肝脏细胞质醛脱氢酶的脱氢酶和酯酶活性作用的进一步研究
Biochem J. 1982 Jun 1;203(3):743-54. doi: 10.1042/bj2030743.

本文引用的文献

1
Isolation and characterization of human liver aldehyde dehydrogenase.
J Biol Chem. 1968 Dec 25;243(24):6402-8.
2
Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity.马肝醛脱氢酶。II. 脱氢酶和酯酶活性的动力学及机制意义。
J Biol Chem. 1972 Jan 10;247(1):267-72.
3
Diphosphopyridine nucleotide-linked aldehyde dehydrogenase. 3. Sulfhydryl characteristics of the enzyme.二磷酸吡啶核苷酸连接的醛脱氢酶。3. 该酶的巯基特性。
Arch Biochem Biophys. 1967 Mar;119(1):253-63. doi: 10.1016/0003-9861(67)90452-3.
4
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.一种利用蛋白质 - 染料结合原理对微克级蛋白质进行定量的快速灵敏方法。
Anal Biochem. 1976 May 7;72:248-54. doi: 10.1016/0003-2697(76)90527-3.
5
The effect of some analogues of disulfiram on the aldehyde dehydrogenases of sheep liver.某些双硫仑类似物对绵羊肝脏醛脱氢酶的影响。
Biochem J. 1976 May 1;155(2):445-8. doi: 10.1042/bj1550445.
6
Studies on the interaction between disulfiram and sheep liver cytoplasmic aldehyde dehydrogenase.双硫仑与羊肝胞质醛脱氢酶相互作用的研究
Biochem J. 1978 Oct 1;175(1):83-90. doi: 10.1042/bj1750083.
7
The separation of sheep liver cytoplasmic and mitochondrial aldehyde dehydrogenases by isoelectric focusing, and observations on the purity of preparations of the cytoplasmic enzyme, and their sensitivity towards inhibition by disulfiram.通过等电聚焦法分离绵羊肝脏细胞质和线粒体醛脱氢酶，以及对细胞质酶制剂纯度及其对双硫仑抑制敏感性的观察。
Biochem J. 1979 Jun 1;179(3):709-12. doi: 10.1042/bj1790709.
8
The disulfiram--ethanol reaction: a review.
J Stud Alcohol. 1977 Jan;38(1):96-113. doi: 10.15288/jsa.1977.38.96.
9
Kinetic properties of aldehyde dehydrogenase from sheep liver mitochondria.绵羊肝脏线粒体中醛脱氢酶的动力学特性
Biochem J. 1978 Dec 1;175(3):899-908. doi: 10.1042/bj1750899.
10
Partial reversal of the acetaldehyde and butyraldehyde oxidation reactions catalysed by aldehyde dehydrogenases from sheep liver.绵羊肝脏醛脱氢酶催化的乙醛和丁醛氧化反应的部分逆转
Biochem J. 1978 Nov 1;175(2):753-6. doi: 10.1042/bj1750753.