Hughes S H, Wahl G M, Capecchi M R
J Biol Chem. 1975 Jan 10;250(1):120-6.
Hypoxanthine-guanine phosphoribosyltransferase (HGPR transferase) (EC 2.4.2.8) has been purified approximately 4500-fold to apparent homogeneity from mouse liver. The procedure involves the use of affinity chromatography and was designed to be readily adaptable to small scale isolations. The enzyme appears to be composed of 3 subunits of identical molecular weight (27,000 per subunit). The subunit molecular weight has also been determined by the analysis of radioactively labeled HGPR transferase immunoprecipitated from wild type and mutant (HGPR transferase) mouse tissue culture cell lines.
次黄嘌呤 - 鸟嘌呤磷酸核糖转移酶（HGPR转移酶）（EC 2.4.2.8）已从小鼠肝脏中纯化出来，纯化倍数约为4500倍，达到了明显的均一性。该方法采用了亲和色谱法，设计用于易于适应小规模分离。该酶似乎由3个分子量相同的亚基组成（每个亚基为27,000）。亚基分子量也通过对从野生型和突变型（HGPR转移酶）小鼠组织培养细胞系中免疫沉淀的放射性标记HGPR转移酶的分析来确定。
