Doronin S V, Lavrik O I, Nevinsky G A, Podust V N
FEBS Lett. 1987 Jun 1;216(2):221-4. doi: 10.1016/0014-5793(87)80693-2.
The interaction of deoxyribonucleoside 5'-mono-, di- and triphosphates with human placenta DNA polymerase alpha was examined. Dissociation constants of enzyme complex formation with dNMP, dNDP and dNTP were determined from the data on enzyme affinity modification by imidazolide of dTMP. The basic role of the primary template-primer interaction with the enzyme in dNTP complex formation is shown. The template-dependent nucleotide interaction does not occur in the case of dNMP and dNDP in comparison with dNTP. The significant contribution of the gamma-phosphate of dNTP in this process is demonstrated.
研究了脱氧核糖核苷5'-单磷酸、二磷酸和三磷酸与人胎盘DNA聚合酶α的相互作用。根据dTMP咪唑酯对酶亲和力修饰的数据，测定了酶与dNMP、dNDP和dNTP形成复合物的解离常数。结果表明，在dNTP复合物形成过程中，初级模板-引物与酶的相互作用起基本作用。与dNTP相比，dNMP和dNDP情况下不发生模板依赖性核苷酸相互作用。结果证明了dNTP的γ-磷酸在这一过程中的重要作用。
