title: Isolation of nuclear acidic proteins from rat tissues. Characterization of acetylated liver nuclear acidic proteins.
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 [(3)H]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 degrees C released 70% of the radioactivity, which indicated that labile acetyl groups had been incorporated into these proteins. Analysis of [(3)H]acetate-labelled nuclear acidic proteins revealed two acetylated amino acid residues, N(2)-acetylserine and N(2)-acetyl-lysine. The significance of the role played by nuclear acidic proteins in relation to gene regulation is discussed.
mesh_terms: D000085:Acetates / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000166:cytology; D001923:Brain Chemistry; D002250:Carbon Radioisotopes; D002467:Cell Nucleus / Q000032:analysis; D002499:Centrifugation, Density Gradient; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000032:analysis / Q000166:cytology; D008099:Liver / Q000032:analysis* / Q000166:cytology; D008297:Male; D008854:Microscopy, Electron; D008858:Microscopy, Phase-Contrast; D009206:Myocardium / Q000032:analysis / Q000166:cytology; D009419:Nerve Tissue Proteins / Q000302:isolation & purification; D009698:Nucleoproteins / Q000302:isolation & purification*; D009928:Organ Specificity; D011487:Protein Conformation; D051381:Rats; D014316:Tritium
chemical_list: D000085:Acetates; D002250:Carbon Radioisotopes; D009419:Nerve Tissue Proteins; D009698:Nucleoproteins; D014316:Tritium