Tavassoli M, Tavassoli M H, Shall S
Eur J Biochem. 1983 Oct 3;135(3):449-55. doi: 10.1111/j.1432-1033.1983.tb07672.x.
Poly(ADP-ribose) glycohydrolase has been purified about 12 300-fold from pig thymus with a recovery of 8.5%. The specific activity of the purified enzyme is 13.8 mumol min -1 mg protein -1. The molecular weight was estimated to be 59 000 by gel filtration through Sephadex G-100 in a non-denaturing solvent. Analysis of the final preparation by sodium dodecyl sulphate gel electrophoresis reveals two protein bands of molecular weight, 61 500 and 67 500. The Km value for poly(ADP-ribose) is estimated to be 1.8 microM monomer units. The enzyme preparation is free from phosphodiesterase, NADase and ADP-ribosyltransferase activities. The purified enzyme is inhibited by cyclic AMP, ADP-ribose, naphthylamine, histones H1, H2A, H2B, H3, polylysine, polyarginine, polyornithine and protamine. The inhibition by histone is relieved by an equal mass of DNA. Single-stranded DNA, poly(A), poly(I) and polyvinyl sulphate were inhibitory, but double-stranded DNA was not inhibitory.
聚（ADP - 核糖）糖水解酶已从猪胸腺中纯化出来，纯化倍数约为12300倍，回收率为8.5%。纯化酶的比活性为13.8 μmol·min⁻¹·mg蛋白质⁻¹。在非变性溶剂中通过Sephadex G - 100凝胶过滤法估计其分子量为59000。用十二烷基硫酸钠凝胶电泳分析最终制剂，显示出分子量分别为61500和67500的两条蛋白带。聚（ADP - 核糖）的Km值估计为1.8 μM单体单元。该酶制剂不含磷酸二酯酶、NAD酶和ADP - 核糖基转移酶活性。纯化酶受到环磷酸腺苷、ADP - 核糖、萘胺、组蛋白H1、H2A、H2B、H3、聚赖氨酸、聚精氨酸、聚鸟氨酸和鱼精蛋白的抑制。组蛋白的抑制作用可被等量的DNA解除。单链DNA、聚（A）、聚（I）和聚乙烯硫酸盐具有抑制作用，但双链DNA没有抑制作用。
