Vicuña R, Valdés F, Medina A, Yudelevich A
J Bacteriol. 1980 Apr;142(1):249-53. doi: 10.1128/jb.142.1.249-253.1980.
A deoxyribonucleic acid (DNA)-dependent DNA polymerase (DNA nucleotidyltransferase) was purified 3,000-fold from the marine Pseuodomonas sp. BAL-31. The molecular weight of the native enzyme was estimated by glycerol gradient sedimentation to be 110,000. The enzyme migrated in sodium dodecyl sulfate-acrylamide gels as a single polypeptide with a molecular weight of 105,000. An absolute requirement for divalent cation was satisfied by Mg2+ or Mn2+ at concentrations of 1 mM. Monovalent cations at concentrations higher than 50 mM showed an inhibitory effect. The polymerase activity was resistant to N-ethylmaleimide and showed a wide pH optimum.
从海洋假单胞菌BAL-31中纯化出一种依赖脱氧核糖核酸（DNA）的DNA聚合酶（DNA核苷酸转移酶），纯化倍数达3000倍。通过甘油梯度沉降法估计该天然酶的分子量为110,000。该酶在十二烷基硫酸钠-丙烯酰胺凝胶中迁移时呈现为一条分子量为105,000的单一多肽。1 mM浓度的Mg2+或Mn2+可满足对二价阳离子的绝对需求。浓度高于50 mM的单价阳离子表现出抑制作用。该聚合酶活性对N-乙基马来酰亚胺具有抗性，且具有较宽的最适pH值。
