Influence of template inactivators on the binding of DNA polymerase to DNA.

Abstract:

: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.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Müller WE,Obermeier J,Totsuka A,Zahn RK

doi

10.1093/nar/1.1.63

keywords:

subject

Has Abstract

pub_date

1974-01-01 00:00:00

pages

63-74

issue

1

eissn

0305-1048

issn

1362-4962

journal_volume

1

pub_type

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