The efficiency of dNTP complex formation with human placenta DNA polymerase α as demonstrated by affinity modification

FEBS Letters

Lavrik, O.I.¹  Doronin, S.V.¹  Podust, V.N.¹  Nevinsky, G.A.¹ 

[1] Institute of Bioorganic Chemistry, Siberian Division of the USSR Academy of Sciences, Novosibirsk 90, USSR

关键词: DNA polymerase α;    Affinity labeling;    dNTP selection;    (Human placenta);    Im-dNMP;    imidazolide of DNMP;    Im-dNTP;    imidazolide of dNTP;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(87)80693-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction of deoxyribonucleoside 5′-mono-, di- and triphosphates with human placenta DNA polymerase α 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 γ-phosphate of dNTP in this process is demonstrated.

【 授权许可】

Unknown