These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A relationship between nuclear poly(adenosine diphosphate ribosylation) and acetylation posttranslational modifications. 1. Nucleosome studies.
    Author: Malik N, Smulson M.
    Journal: Biochemistry; 1984 Jul 31; 23(16):3721-5. PubMed ID: 6089879.
    Abstract:
    The chromatin-associated enzyme poly(ADP-Rib) polymerase catalyzes the posttranslational modifications of histones. Antibody to poly(adenosine diphosphate ribose) [poly(ADP-Rib)] has been coupled to Sepharose, and the resulting immunoadsorbant was used to fractionate, specifically, oligonucleosomes derived from cells pulse labeled for the acetylation modifications of chromatin by incubation with [3H]acetate followed by treatment with sodium butyrate. Generally, about 50% of the histone H3 and H4 mass becomes acetylated under these conditions. Pulse-labeled acetylated regions of chromatin were selectively retained by the anti-poly(ADP-Rib)-Sepharose column due to the presence of endogenous poly(ADP-Rib) components. The data suggest that certain histone molecules might be mutally poly(ADP-ribosylated) and acetylated, and this phenomenon was further explored at the protein level in the accompanying paper [Wong, M., & Smulson, M. (1984) Biochemistry (following paper in this issue)].
    [Abstract] [Full Text] [Related] [New Search]