Kahn R A, Gilman A G
J Biol Chem. 1984 May 25;259(10):6228-34.
A factor (ARF) that is required for the cholera toxin-dependent ADP-ribosylation of the stimulatory, GTP-binding regulatory component (Gs) of adenylate cyclase has been purified about 2000-fold from cholate extracts of rabbit liver membranes. ARF is an intrinsic membrane protein with Mr = 21,000. The final product can be resolved into two polypeptides with very similar molecular weights; each of these has ARF activity. The ADP-ribosylation of Gs can now be studied with defined components. GTP and ARF are both necessary cofactors. The data imply that the substrates for the activated toxin are NAD and a GTP X Gs X ARF complex, and the reaction proceeds in a lipid environment. The apparent ability of ARF to bind to the alpha subunit of Gs suggests that it may play another, unknown role in the regulation of adenylate cyclase activity.
一种参与霍乱毒素依赖的腺苷酸环化酶刺激性GTP结合调节成分（Gs）的ADP核糖基化反应的因子（ARF），已从兔肝细胞膜的胆酸盐提取物中纯化了约2000倍。ARF是一种分子量为21,000的内在膜蛋白。最终产物可分解为两种分子量非常相似的多肽；每一种都具有ARF活性。现在可以用确定的成分来研究Gs的ADP核糖基化反应。GTP和ARF都是必需的辅助因子。数据表明，活化毒素的底物是NAD和GTP·Gs·ARF复合物，并且反应在脂质环境中进行。ARF与Gs的α亚基结合的明显能力表明，它可能在腺苷酸环化酶活性的调节中发挥另一种未知作用。
