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Covalent modification of nuclear proteins during aging

  • C. C. Liew
  • A. G. Gornall
Part of the Faseb Monographs book series (FASEBM, volume 3)

Abstract

An in vitro assay system has been established to study acetylation and phosphorylation of nuclear proteins from isolated nuclei. Phosphorylation of nuclear proteins reached a peak within 5 min while maximum acetylation occurred about 10 min later. The rate of acetylation of liver nuclear proteins in 15 min incubation was significantly higher in ‘old’ mice (29 mo) than in ‘young’ mice (2 mo), while there was no difference in phosphorylation. When nuclear histones were fractionated by polyacrylamide-urea electrophoresis the acetylation of histone F3 was increased in ‘old’ mice to 129% and F2a1 to 112% of the values in ‘young’ mice. Acetylation of phenol-soluble nuclear acidic proteins was increased to 250% phosphorylation to 138% in ‘old’ mice as compared to ‘young’ mice. This increase in covalent modification of acidic proteins was found in two specific fractions when separated by SDS-polyacrylamide gel electrophoresis. By contrast, the labeling of nucleoplasmic proteins, soluble in 0.14 M NaCI, showed no significant difference between the two ages.—Liew, C. C. and A. G. GORNALL. Covalent modification of nuclear proteins during aging. Federation Proc. 34: 186–187, 1975.

Keywords

Nuclear Protein Covalent Modification Specific Fraction Liver Nucleus Filter Paper Strip 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Federation of American Societies 1975

Authors and Affiliations

  • C. C. Liew
    • 1
  • A. G. Gornall
    • 1
  1. 1.Department of Clinical Biochemistry Banting Institute Faculty of MedicineUniversity of TorontoTorontoCanada

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