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. 2011:780:209-26.
doi: 10.1007/978-1-61779-270-0_13.

Purification of human PARP-1 and PARP-1 domains from Escherichia coli for structural and biochemical analysis

Marie-France Langelier  1 , Jamie L Planck, Kristin M Servent, John M Pascal
Affiliations

Purification of human PARP-1 and PARP-1 domains from Escherichia coli for structural and biochemical analysis

Marie-France Langelier et al. Methods Mol Biol. 2011.

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.

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