Showing papers on "Polyamine binding published in 1979"
TL;DR: A possible mechanism of promotion of DNA transcription by polyamines is discussed in connection with their stabilizing effect on the Ā conformation of DNA.
89 citations
TL;DR: The protein, which is named α-protein, is a cytosol protein which binds certain steroids weakly and is also found in the secretory fluid of the ventral prostate and appears to be identical with the “prostatein” or ”prostate-binding protein” studied recently by other investigators.
44 citations
TL;DR: When rat liver nuclei prepared with polyamines as stabilising cations are digested with DNAase II, release of both inactive chromatin and Mg-soluble, active chromatin is greatly reduced, in comparison to digestion of liver nuclea prepared with Mg2+ as stabilisation cation.
Abstract: When rat liver nuclei prepared with polyamines as stabilising cations are digested with DNAase II, release of both inactive chromatin and Mg-soluble, active chromatin is greatly reduced, in comparison to digestion of liver nuclei prepared with Mg2+ as stabilising cation. Chromatin release from polyamine stabilised nuclei is also inhibited relative to Mg-stabilised nuclei following digestion with micrococcal nuclease under two very different cation conditions. Nuclei prepared with polyamines and monovalent ions as stabilising cations exhibit properties intermediate between these two extremes with both nucleases. These effects are due to residual binding of polyamines to chromatin, which is thus maintained in a condensed state, inaccessible to nucleases. Since polyamine binding is not easily reversed, concentrations of polyamines and other cations must be rigidly controlled in experiments on chromatin structure if artefacts are to be avoided. The significance of these findings to the nature and properties of active chromatin within the intact nucleus is considered.
29 citations
TL;DR: In this paper, it was shown that ruthenium red acts as a paramagnetic probe in NMR spectroscopy, and that it can be used as a substitution probe for polyamine binding sites in biological systems.