Mozzherin D Iu, Atrazhev A M, Kukhanova M K
Mol Biol (Mosk). 1992 Sep-Oct;26(5):999-1010.
DNA polymerase epsilon was purified to near homogeneity from human placenta. The enzyme has one subunit (170 kDa, sedimentation coefficient 8.2S), intrinsic 3'-5'-exonuclease activity, it is independent on PCNA and high processivity on poly(dA)-oligo(dT) template-primer without PCNA. It was shown, that the enzyme incorporates 3'-amino-2',3'-dideoxythymidine 5'-triphosphate in DNA, after that synthesis is stopped. Simultaneously DNA polymerase alpha was purified.
从人胎盘中将DNA聚合酶ε纯化至接近均一状态。该酶有一个亚基(170 kDa,沉降系数8.2S),具有内在的3'-5'-外切核酸酶活性,不依赖增殖细胞核抗原(PCNA),在没有PCNA的情况下对聚(dA)-寡聚(dT)模板引物具有高持续合成能力。结果表明,该酶将3'-氨基-2',3'-双脱氧胸苷5'-三磷酸掺入DNA后,合成即停止。同时,对DNA聚合酶α进行了纯化。