Ramponi G, Manao G, Camici G
Biochemistry. 1975 Jun 17;14(12):2681-5. doi: 10.1021/bi00683a018.
Nonenzymatic acetylation of calf-thymus lysine- and arginine-rich histones was demonstrated to occur when these proteins were incubated with [14C]acetyl phosphate and [14C]acetyl adenylate. The levels of acetylation depend on both pH and on reagent concentration. When acetyl [33P]phosphate and acetyl [3H]adenylate were used as reagents, we found neither histone phosphorylation nor adenylylation. Most of the radioactivity of 14C-labeled acetylated histones was recovered as Ne-acetyllysine. Furthermore, only a small amount of O-bound radioactivity was released by the 14C-labeled acetylated arginine-rich histone during treatment with hydroxylamine. Experiments on the acetylation of histones, in the presence of increasing salt concentration, gave different results for the two acetylating agents.
当用[14C]乙酰磷酸和[14C]乙酰腺苷酸孵育小牛胸腺富含赖氨酸和精氨酸的组蛋白时，可证明发生了非酶促乙酰化。乙酰化水平取决于pH值和试剂浓度。当使用乙酰[33P]磷酸和乙酰[3H]腺苷酸作为试剂时，我们既未发现组蛋白磷酸化也未发现腺苷酸化。14C标记的乙酰化组蛋白的大部分放射性以Nε-乙酰赖氨酸形式回收。此外，在用羟胺处理期间，14C标记的富含精氨酸的乙酰化组蛋白仅释放少量与氧结合的放射性。在盐浓度增加的情况下对组蛋白乙酰化进行的实验，对于两种乙酰化试剂给出了不同的结果。
