| Literature DB >> 21870263 |
Marie-France Langelier1, Jamie L Planck, Kristin M Servent, John M Pascal.
Abstract
A general method to express and purify full-length human poly(ADP-ribose) polymerase-1 (PARP-1), individual PARP-1 domains, and groups of PARP-1 domains from Escherichia coli cells is described. The procedure allows for robust production of highly pure PARP-1 that is free of DNA contamination and well-suited for biochemical experiments and for structural and biophysical analysis. Two biochemical assays for monitoring PARP-1 automodification activity are presented that can be used to evaluate purified PARP-1, combinations of PARP-1 domains, or PARP-1 mutants.Entities:
Mesh:
Substances:
Year: 2011 PMID: 21870263 DOI: 10.1007/978-1-61779-270-0_13
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745