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. 1974 Feb;137(2):355–362. doi: 10.1042/bj1370355

Isolation of nuclear acidic proteins from rat tissues. Characterization of acetylated liver nuclear acidic proteins

D Suria 1, C C Liew 1
PMCID: PMC1166124  PMID: 4596143

Abstract

Nuclear acidic proteins isolated from rat brain, heart, kidney and liver showed similar, complex patterns on electrophoresis in sodium dodecyl sulphate–polyacrylamide gels. The contamination of nuclear acidic proteins by nuclear-membrane acidic proteins was found to the extent of 11%. Incorporation of [3H]acetate into the various nuclear acidic proteins in vivo, which were fractionated by polyacrylamide-gel electrophoresis, differed from tissue to tissue. Hydrolysis of these acetylated nuclear acidic proteins with 6m-HCl at 110°C released 70% of the radioactivity, which indicated that labile acetyl groups had been incorporated into these proteins. Analysis of [3H]acetate-labelled nuclear acidic proteins revealed two acetylated amino acid residues, N2-acetylserine and N2-acetyl-lysine. The significance of the role played by nuclear acidic proteins in relation to gene regulation is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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