1,721,010 research outputs found

    Flow cytometric analysis of liposome‐nuclei interaction: Transfer and intranuclear release of carboxyfluorescein

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    Flow cytometric analysis of the transfer of liposome-encapsulated carboxyfluorescein to isolated rat liver nuclei indicated that the fluorophore is actively taken up in this form, while negligible amounts are transferred when the dye is free in the reaction medium. The kinetic analysis of the uptake indicated a time- and dose-dependent reduction of the slope in the absence of transport saturable sites on the nuclear surface and of quenching phenomena. The comparison between entire and membrane-deprived nuclei demonstrated that the initial rate of uptake was higher in the absence of the complete nuclear envelope. The intranuclear binding sites were considered on the basis of the fluorescence distribution and of quantitative estimates of the amount of linked dye. The possibility of employing flow cytometry to monitor the interactions between liposomes and isolated nuclei by means of a fluorescent probe is discussed

    1H-NMR RELAXATION STUDY OF THE LIPOSOME - NUCLEI INTERACTION

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    Phospholipidic liposomes can influence DNA template availability for RNA synthesis when interacting with isolated nuclei by enhancing (when the phospholipids are negatively charged) or by inhibiting (when they are neutral) trascriptional activity. The analysis of the 1H-NMR relaxation behaviour of isolated nuclei, of Small Unilamellar Vesicles (SUV) and of the SUV-Nuclei system has been undertaken to elucidate the mechanism of the interaction between the nuclear core and the phospholipids

    Phospholipids as components of the nuclear matrix: their possible biological significance.

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    The phospholipid involvement in the regulation of the functional and structural properties of the nuclear matrix is discussed analysing the results obtained with the enzymic removal of these molecules. Namely phospholipids seem to mediate hydrophobic interactions between nucleic acids and matrix fibrils either directly or indirectly through an association with the non-histone proteins of the matrix
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