Wintersberger E
Eur J Biochem. 1978 Mar;84(1):167-72. doi: 10.1111/j.1432-1033.1978.tb12153.x.
Highly purified preparation of DNA polymerases A and B from yeast were compared with respect to antigenic relationship, ability to use ribonucleotide primers and associated nuclease activity. The following results were obtained. 1. Antiserum directed against DNA polymerase A inhibits this enzyme but does not interfere with activity of DNA polymerase B or of mitochondrial DNA polymerase, nor does it precipitate the latter two enzymes. 2. DNA polymerase A is capable of using oligo(ribouridylic acid) as a primer for the polymerization of dTMP. This reaction is not catalyzed by polymerase B to any significant extent. 3. Whereas DNA polymerase A is devoid of nuclease activity, DNA polymerase B catalyses an exonucleolytic release of mononucleotide units from the 3' end of polynucleotides. The results of several experiments suggest that this nuclease activity is associated with the DNA polymerase B molecule.
对从酵母中高度纯化得到的DNA聚合酶A和B在抗原关系、使用核糖核苷酸引物的能力以及相关核酸酶活性方面进行了比较。得到了以下结果。1. 针对DNA聚合酶A的抗血清抑制该酶，但不干扰DNA聚合酶B或线粒体DNA聚合酶的活性，也不会沉淀后两种酶。2. DNA聚合酶A能够使用寡聚（核糖尿苷酸）作为dTMP聚合的引物。该反应在很大程度上不会被聚合酶B催化。3. 虽然DNA聚合酶A没有核酸酶活性，但DNA聚合酶B催化从多核苷酸3'末端以核酸外切方式释放单核苷酸单元。几个实验的结果表明这种核酸酶活性与DNA聚合酶B分子相关。
