@article{74416850b70f49d2a8ad9ed7c8af71fb,
title = "A rapid and sensitive assay for histone acetyl-transferase activity",
abstract = "Histone acetyl-transferases (HATs) seem to be key elements in the regulation of transcription. We have designed an enzymatic assay to quantify HAT enzymatic activity. In this assay, the substrate is a peptide corresponding to the 24 first amino acids of histone H4 which is coupled to biotin. After acetylation using [14C]acetyl-CoA, the peptide is purified on streptavidin beads and the associated radioactivity is measured. This assay is sensitive, rapid and convenient.",
author = "S. Ait-Si-Ali and S. Ramirez and P. Robin and D. Trouche and A. Harel-Bellan",
note = "Funding Information: This work was supported by grants from the Ligue Nationale contre le Cancer, the Comit{\'e} de l{\textquoteright}Essone, the Comit{\'e} du Val de Marne, the Comit{\'e} des Yvelines of the Ligue Nationale contre le Cancer and from the Association pour la Recherche sur le Cancer. S.A. was a recipient of a fellowship from the Comit{\'e} de la Haute-Sa{\^o}ne of the Ligue Nationale contre le Cancer. S.R. was a recipient of a travel award from the Colombian Government (Colcencias). The authors wish to thank Chiron for their help in the design and the synthesis of the peptide and Linda L. Pritchard for critical reading of the manuscript.",
year = "1998",
month = aug,
day = "15",
doi = "10.1093/nar/26.16.3869",
language = "English (US)",
volume = "26",
pages = "3869--3870",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "16",
}