骨骼肌中一种水解与蛋白质结合的ADP-核糖的酶活性的鉴定。

Identification of an enzymatic activity that hydrolyzes protein-bound ADP-ribose in skeletal muscle.

作者信息

Chang Y C, Soman G, Graves D J

出版信息

Biochem Biophys Res Commun. 1986 Sep 30;139(3):932-9. doi: 10.1016/s0006-291x(86)80267-4.

Abstract

An enzymatic activity present in high-speed supernatant fluids of rat skeletal muscle was found that catalyzes the release of ADP-ribose from ADP-ribosylated-modified lysozyme. The nature of the product was proved by chromatographic studies and proton nuclear magnetic resonance spectroscopy. The enzyme activity is stimulated by Mg2+, dithioerythritol, and flouride. These results and those published earlier (Soman, G., Mickelson, J.R., Louis, C.F., and Graves, D.J. (1984) Biochem. Biophys. Res. Commun. 120, 973-980) show that ADP-ribosylation is a reversible process in skeletal muscle.

摘要

在大鼠骨骼肌高速上清液中发现了一种酶活性，它能催化ADP-核糖基化修饰的溶菌酶释放ADP-核糖。通过色谱研究和质子核磁共振光谱证实了产物的性质。该酶活性受到Mg2+、二硫苏糖醇和氟化物的刺激。这些结果以及早期发表的结果（索曼，G.，米克尔森，J.R.，路易斯，C.F.，和格雷夫斯，D.J.（1984年）《生物化学与生物物理学研究通讯》120，973 - 980）表明，ADP-核糖基化在骨骼肌中是一个可逆过程。