Suppr超能文献

大鼠肝脏线粒体内膜中的ADP核糖基化作用。

ADP-ribosylation in inner membrane of rat liver mitochondria.

作者信息

Richter C, Winterhalter K H, Baumhüter S, Lötscher H R, Moser B

出版信息

Proc Natl Acad Sci U S A. 1983 Jun;80(11):3188-92. doi: 10.1073/pnas.80.11.3188.

Abstract

NAD+ glycohydrolase activity is found at high levels in submitochondrial particles. It leads to the reaction products ADP-ribose, nicotinamide, and small amounts of 5'-AMP. Furthermore, submitochondrial particles catalyze the exchange reaction: [adenosine-14C]ADP-ribose + NAD+ in equilibrium [adenosine-14C]-NAD+ + ADP-ribose. When submitochondrial particles are incubated with NAD+, mono(ADP-ribosyl)ation of protein molecules migrating with an apparent molecular weight of 30,000 in sodium dodecyl sulfate/polyacrylamide gel electrophoresis is demonstrable. Inhibitor studies suggest attachment of ADP-ribose to arginine residues. ADP-ribose bound to submitochondrial particles is rapidly turning over. The release of ADP-ribose from the protein is probably enzyme catalyzed. The rapid turnover, the specificity of the modification, and the inhibition of ADP-ribosylation by ATP and nicotinamide suggest a regulatory role of mono(ADP-ribosyl)ation of a protein in the inner mitochondrial membrane.

摘要

在线粒体亚颗粒中发现了高水平的NAD + 糖水解酶活性。它会产生反应产物ADP-核糖、烟酰胺和少量的5'-AMP。此外,线粒体亚颗粒催化交换反应:[腺苷-14C]ADP-核糖 + NAD + 处于平衡状态 [腺苷-14C]-NAD + + ADP-核糖。当线粒体亚颗粒与NAD + 一起孵育时,在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳中可证明表观分子量为30,000的蛋白质分子发生了单(ADP-核糖基)化。抑制剂研究表明ADP-核糖与精氨酸残基相连。与线粒体亚颗粒结合的ADP-核糖迅速周转。ADP-核糖从蛋白质上的释放可能是酶催化的。快速周转、修饰的特异性以及ATP和烟酰胺对ADP-核糖基化的抑制表明线粒体内膜中蛋白质的单(ADP-核糖基)化具有调节作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d72c/394005/9063169168bf/pnas00637-0055-a.jpg

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验