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The efficiency of dNTP complex formation with human placenta DNA polymerase α as demonstrated by affinity modification
Author(s) -
Doronin S.V.,
Lavrik O.I.,
Nevinsky G.A.,
Podust V.N.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80693-2
Subject(s) - deoxyribonucleoside , enzyme , chemistry , polymerase , dna , dna polymerase , human placenta , dissociation constant , nucleotide , primer (cosmetics) , biochemistry , dissociation (chemistry) , placenta , stereochemistry , microbiology and biotechnology , biology , gene , genetics , receptor , organic chemistry , fetus , pregnancy
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.