Inactivation of DNA polymerases by adenosine 2′,3′-riboepoxide 5′-triphosphate allows estimation of the primers affinity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-11

AUTHORS

Vladimir N. Podust, Tamara O. Korobeinicheva, George A. Nevinsky, Asja S. Levina, Olga I. Lavrik

ABSTRACT

Template-primer dependent inactivation of human DNA polymerase alpha and Klenow fragment of E. coli DNA polymerase I by adenosine 2',3'-riboepoxide 5'-triphosphate was used for quantitative analysis of the Kd values for oligonucleotide primers of different length. The Kd values are smaller by a factor of 2.5 than the Km values for the same primers determined in the reaction of DNA polymerization in the case of DNA polymerase alpha. The Kd and Km values are nearly the same for Klenow fragment. Such approach to the determination of Km/Kd ratio can likely be used for detailed quantitative analysis of DNA polymerases. More... »

PAGES

247-249

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00429892

DOI

http://dx.doi.org/10.1007/bf00429892

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014888625

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1710018


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