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Toxic effects of lead and nickel nitrate on rat liver chromatin components.

Journal of biochemical and molecular toxicology (2011-06-15)
Azra Rabbani-Chadegani Iii, Nesa Fani, Sayeh Abdossamadi, Nosrat Shahmir
ABSTRACT

The biological activity of heavy metals is related to their physicochemical interaction with biological receptors. In the present study, the effect of low concentrations of nickel nitrate and lead nitrate (<0.3 mM) on rat liver soluble chromatin and histone proteins was examined. The results showed that addition of various concentrations of metals to chromatin solution preceded the chromatin into aggregation and precipitation in a dose-dependant manner; however, the extent of absorbance changes at 260 and 400 nm was different between two metals. Gel electrophoresis of histone proteins and DNA of the supernatants obtained from the metal-treated chromatin and the controls revealed higher affinity of lead nitrate to chromatin compared to nickel nitrate. Also, the binding affinity of lead nitrate to histone proteins free in solution was higher than nickel. On the basis of the results, it is concluded that lead reacts with chromatin components even at very low concentrations and induce chromatin aggregation through histone-DNA cross-links. Whereas, nickel nitrate is less effective on chromatin at low concentrations, suggesting higher toxicity of lead nitrate on chromatin compared to nickel.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Nickel(II) nitrate hexahydrate, 99.999% trace metals basis
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Lead(II) nitrate, ACS reagent, ≥99.0%
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Nickel(II) nitrate hexahydrate, crystals or chunks
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Lead(II) nitrate, 99.999% trace metals basis
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Nickel(II) nitrate hexahydrate, purum p.a., crystallized, ≥97.0% (KT)
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Nickel(II) nitrate hexahydrate, puriss. p.a., ≥98.5% (KT)
Sigma-Aldrich
Lead(II) nitrate, ≥99.95% trace metals basis