Baldi M I, Bazzicalupo P, Tocchini-Valentini G P
Laboratory of Cell Biology, C. N. R., Via Romagnosi 18A, 00196 Rome, Italy.
Biochem Biophys Res Commun. 1976 Dec 20;73(4):985-92. doi: 10.1016/0006-291x(76)90219-9.
A DNA polymerase has been partially purified and characterized from Xenopus laevis stage 6 oocytes. The enzyme is present only in the cytoplasm and has been shown to be able to copy Poly(A) x oligo(dT), to be sensitive to N-ethylmaleimide, and to sediment faster than 4 S in high salt glycerol gradient. The enzyme can be extracted from particulate material which has a density in sucrose gradient ranging from 1.200 to 1.225 g/cc. This particulate material is identified by its ability to use Poly(A) x oligo(dT) as template in an exogenous DNA polymerase reaction and by its endogenous DNA synthesizing capacity.
已从非洲爪蟾6期卵母细胞中部分纯化并鉴定出一种DNA聚合酶。该酶仅存在于细胞质中，已证明它能够复制聚腺苷酸x寡聚脱氧胸苷酸，对N-乙基马来酰胺敏感，并且在高盐甘油梯度中沉降速度快于4S。该酶可从蔗糖梯度中密度为1.200至1.225g/cc的颗粒物质中提取。这种颗粒物质通过其在外源DNA聚合酶反应中使用聚腺苷酸x寡聚脱氧胸苷酸作为模板的能力及其内源性DNA合成能力来鉴定。
