0000000001002214
AUTHOR
Jürgen Obermeier
Poly(adenosine diphosphate-ribose) polymerase in quail oviduct. Changes during estrogen and progesterone induction
Abstract The activities of the following enzymes have been determined in nuclei of quail oviducts in response to exogenous stimulation of the birds with diethylstilbestrol, used as an estrogen analogue and progesterone: DNA dependent DNA polymerase, DNA dependent RNA polymerase I and II and poly(adenosine diphosphate-ribose) [=poly(ADP-Rib)] polymerase. During primary stimulation with the estrogen analogue the activities of the four DNA dependent polymerases increase to about the same degree. Upon withdrawal of the hormones the levels of the enzymes drop to values known from nuclei from unstimulated quail oviducts. The secondary stimulation with the estrogen analogue causes a significant in…
Influence of template inactivators on the binding of DNA polymerase to DNA.
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 …