Kaledin A S, Sliusarenko A G, Gorodetskiĭ S I
Biokhimiia. 1982 Nov;47(11):1785-91.
A DNA-polymerase from the external thermophylic bacteria Thermus ruber has been isolated. A six-step purification procedure resulted in an electrophoretically homogeneous enzyme preparation with m. w. of 70 000. The isolated enzyme is thermostable and has a temperature optimum on DNA templates at 70 degrees and that on RNA templates at 50 degrees. The enzyme does not contain contaminant endo- and exonuclease activities. The maximal activity of the enzyme requires the presence of template, four deoxyribonucleoside triphosphates, monovalent and divalent cations in the incubation mixture. The catalytic activity of the enzyme on various templates of DNA- and RNA-types has been investigated. A comparative physico-chemical study of this DNA-polymerase and an analogous enzyme isolated earlier from the external thermophylic bacteria Thermus aquaticus YT-1 has been carried out.
已从嗜热细菌红栖热放线菌中分离出一种DNA聚合酶。经过六步纯化程序,得到了一种电泳纯的酶制剂,其分子量为70000。分离出的酶具有热稳定性,在DNA模板上的最适温度为70℃,在RNA模板上的最适温度为50℃。该酶不含有污染性的内切酶和外切酶活性。酶的最大活性要求在孵育混合物中存在模板、四种脱氧核糖核苷三磷酸、一价和二价阳离子。已经研究了该酶对各种DNA型和RNA型模板的催化活性。对这种DNA聚合酶和先前从嗜热细菌嗜热水生栖热放线菌YT-1中分离出的类似酶进行了比较物理化学研究。