Bezuglyĭ S V, Skripal' I G, Babichev V V
Mikrobiol Zh (1978). 1992 Jan-Feb;54(1):51-7.
The DNA-dependent DNA-polymerase (DNA polymerase I which is not sorbed on the column with DEAE-cellulose, and DNA-polymerase II, which is absorbed by this column and is eluted from it by 0.3 M of NaCl), have been isolated from Acholeplasma laidlawii PG-8. DNA-polymerase I in homogeneous state was obtained as a result of the stepwise treatment by heparin-sepharose (elution at 0.35 M of NaCl) and poly-U-sepharose (elution at 0.3 M of NaCl). It was presented on the electrophoregram by one polypeptide with molecular weight of 72 kDalton. The second form of DNA polymerase was also obtained in homogeneous state as a result of sequential treatment on heparin-sepharose (elution at 0.3 M of NaCl) and on poly-A-sepharose (elution at 0.25 M of NaCl): the protein which had manifested polymerase activity was a polypeptide with molecular weight of 45 kDalton.
已从莱氏无胆甾原体PG - 8中分离出DNA依赖性DNA聚合酶（不被DEAE - 纤维素柱吸附的DNA聚合酶I和被该柱吸附并被0.3M NaCl洗脱的DNA聚合酶II）。通过肝素 - 琼脂糖（在0.35M NaCl下洗脱）和聚 - U - 琼脂糖（在0.3M NaCl下洗脱）的逐步处理，获得了均一状态的DNA聚合酶I。在电泳图谱上，它由一条分子量为72千道尔顿的多肽表示。通过对肝素 - 琼脂糖（在0.3M NaCl下洗脱）和聚 - A - 琼脂糖（在0.25M NaCl下洗脱）的顺序处理，也获得了均一状态的第二种形式的DNA聚合酶：表现出聚合酶活性的蛋白质是一条分子量为45千道尔顿的多肽。
