The efficiency of dNTP complex formation with human placenta DNA polymerase α as demonstrated by affinity modification
- 1 June 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 216 (2) , 221-224
- https://doi.org/10.1016/0014-5793(87)80693-2
Abstract
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.Keywords
This publication has 4 references indexed in Scilit:
- TROPOLONEOrganic Syntheses, 1977
- The Mechanism of Escherichia coli Deoxyribonucleic Acid Polymerase IPublished by Elsevier ,1972
- Enzymatic Synthesis of Deoxyribonucleic AcidPublished by Elsevier ,1970
- Enzymatic Synthesis of Deoxyribonucleic AcidJournal of Biological Chemistry, 1969