| Literature DB >> 21870260 |
Jennifer E Rood1, Anthony K L Leung, Paul Chang.
Abstract
Poly(ADP-ribose) (pADPr) is a posttranslational modification that regulates protein function through two major mechanisms: covalent modification of acceptor proteins and noncovalent binding of proteins to pADPr. pADPr is synthesized by a family of enzymes called poly(ADP-ribose) polymerases (PARPs) that are themselves major targets of pADPr modification. Here, we outline two methods for the purification of pADPr-binding proteins via pADPr purification under native conditions: purification of cellular pADPr and pADPr covalently linked to specific PARPs. Together, these methods provide complementary approaches to the identification of noncovalent pADPr-protein interactions in the cell.Entities:
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Year: 2011 PMID： 21870260 PMCID： PMC3494285 DOI： 10.1007/978-1-61779-270-0_10
Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745