| Literature DB >> 28843507 |
Tasha B Toro1, Richard G Painter2, Rashad A Haynes3, Elena Y Glotser4, Melyssa R Bratton5, Jenae R Bryant6, Kyara A Nichols7, Asia N Matthew-Onabanjo8, Ashley N Matthew9, Derek R Bratcher10, Chanel D Perry11, Terry J Watt12.
Abstract
Metal-dependent lysine deacetylases (KDACs) are involved in regulation of numerous biological and disease processes through control of post-translational acetylation. Characterization of KDAC activity and substrate identification is complicated by inconsistent activity of prepared enzyme and a range of multi-step purifications. We describe a simplified protocol based on two-step affinity chromatography. The purification method is appropriate for use regardless of expression host, and we demonstrate purification of several representative members of the KDAC family as well as a selection of mutated variants. The purified proteins are highly active and consistent across preparations.Entities:
Keywords: Histone deacetylase; Lysine deacetylase; hdac
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Year: 2017 PMID： 28843507 PMCID： PMC5624855 DOI： 10.1016/j.pep.2017.08.009
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650