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RESEARCH PRODUCT
Influence of template inactivators on the binding of DNA polymerase to DNA.
Jürgen ObermeierRudolf K. ZahnWerner E. G. M�llerAtsuko Totsukasubject
MaleDNA polymeraseDNA polymerase IICytochrome c GroupIn Vitro Techniqueschemistry.chemical_compoundNucleic acid thermodynamicsEthidiumGeneticsAnimalsEnzyme InhibitorsPolymeraseDNA clampBinding SitesbiologyDaunorubicinDistamycinsDNADNA Polymerase IMolecular biologyKineticschemistryBiochemistrybiology.proteinPrimer (molecular biology)DNA polymerase IDNAdescription
The agents daunomycin, ethidium bromide, distamycin A and cytochrome c inhibit DNA dependent DNA polymerase I (E. coli) reaction competitively to DNA. The influence of these template inactivators on the binding of DNA polymerase to native as well as denatured DNA has been determined by affinity chromatography. Cytochrome c blocks the binding of the enzyme to double-stranded and to single-stranded DNA Sepharose. In contrast to these results daunomycin, ethidium bromide or distamycin A reduce the binding affinity only with denatured DNA Sepharose as matrix. These data are discussed with respect to the modification by template inactivators of the affinity of DNA to the different binding sites of the DNA polymerase.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1974-01-01 | Nucleic acids research |