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Nucleic Acids Research, 1981, Vol. 9, No. 21 5811-5824
© 1981

CHEMISTRY

Partitioning of zinc and copper within subnuclear nucleoprotein particles

Sara E. Bryan*, Douglas L. Vizard+, David A. Beary, Ronald A. LaBiche and Kenneth J. Hardy

Department of Biological Sciences, University of New Orleans New Orleans, LA 70122 +Department of Physics, The University of Texas System Cancer Center, M.D.Anderson Hospital and Tumor Institute Houston, TX 77030, USA

*Author to whom all correspondence should be sent.

Received August 13, 1981. Nuclei from frozen calf thymus suspended in buffer were analyzed for metal content prior to and after repeated washing. After three such extractions about 0.1 µg Zn/mg DNA and 0.025 µg Cu/mg DNA remained tightly associated with chromatin. This level of metal was essentially unchanged with subsequent washings. Digestion of extracted nuclei with micrococcal nuclease yielded soluble nucleoprotein containing zinc and copper. Metal enriched regions of chromatin appeared to be preferentially solubilized by digestion, and the solubilized metal was only partially dializable either with or without EDTA. Metal profiles generated from gel (A-5m) chromatography analysis of chelated and non-chelated solubilized chromatin were distinctive in that copper was undetectable (by flame AA) while zinc was associated only with low molecular weight products when EDTA was used. In contrast, both metals were detected with higher molecular weight oligonucleosomes in the absence of chelating agents. Additionally, the two metals localized within nucleoprotein peaks and these metal-containing regions were only resolved by gel chromatography when EDTA was omitted throughout the procedure. A discrete Cu-rich species in a region of the profile suggests a subset of Cu-rich nucleoprotein complexes.


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