Kobayashi Y, Kuratomi K
Biochem Biophys Res Commun. 1983 Apr 15;112(1):80-7. doi: 10.1016/0006-291x(83)91800-4.
A fraction (P1) which showed DNA polymerase III holoenzyme activity was obtained by partial purification including Polymin P fractionation from extracts of E. coli K-12 wild type (pol A+, pol B+) cells. The P1 fraction was composed of three macromolecular complexes, 11 S, 18 S and 24 S, all of which possessed holoenzyme activity. The activity of the P1 fraction was maximal at about 70 mM NaCl. The synthesis of long-chain poly(dT) with a poly(dA) oligo(dT)10 primer was dependent on the presence of ATP, but not on the presence of spermidine, suggesting that the single-stranded DNA binding protein (SSB) was present in the fraction. The intermediate lengths of the products in the absence of ATP and NaCl also suggest the functioning of DNA polymerase III'.
通过对大肠杆菌K-12野生型（pol A+，pol B+）细胞提取物进行包括聚胺P分级分离在内的部分纯化，获得了具有DNA聚合酶III全酶活性的一个组分（P1）。P1组分由三种大分子复合物组成，分别为11 S、18 S和24 S，它们均具有全酶活性。P1组分的活性在约70 mM NaCl时最大。以聚（dA）寡聚（dT）10为引物合成长链聚（dT）依赖于ATP的存在，但不依赖于亚精胺的存在，这表明该组分中存在单链DNA结合蛋白（SSB）。在没有ATP和NaCl的情况下产物的中间长度也表明了DNA聚合酶III的功能。
