Effects of various ionic media on extraction of soluble nuclear proteins and on nuclear ultrastructure

  • Kellermayer M
  • Olson M
  • Smetana K
 et al. 
  • 2

    Readers

    Mendeley users who have this article in their library.
  • 16

    Citations

    Citations of this article.

Abstract

Isolated liver nuclei were extracted 3 times at pH 7.2 with solutions containing either (1) monovalent cations, (2) both mono- and divalent cations, or (3) sucrose solutions containing only divalent cations. The extracted proteins were analysed by two-dimensional acrylamide gel electrophoresis and the ultrastructural alterations of the treated nuclei were examined by electron microscopy. The solutions containing Na+or K+monovalent and Ca2+and Mg2+divalent ions extracted the same amount (18-22 %) of the nuclear proteins. The two-dimensional gel electrophoretic patterns of these extracts were nearly identical and the structures of the nuclear components were well preserved even after 3 times repeated extractions. The solution containing only Na+extracted less protein (14-15 %) than the solutions containing both mono- and divalent cations. Extraction with isotonic NaCl solution altered the nuclear and nucleolar morphology; unlike the other solutions employed, this solution extracted some DNA and histones. The isotonic sucrose solution containing only divalent cations extracted less protein than the other solutions (9-11 %) and produced marked condensation of the chromatin. These analytical and electron microscopic studies showed that mono- and divalent cations play a role in structural organization of chromatin. © 1974.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • M. Kellermayer

  • M. O.J. Olson

  • K. Smetana

  • I. Daskal

  • H. Busch

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free