Solubilization and purification of recombinant modified C-reactive protein from inclusion bodies using reversible anhydride modification.

ABSTRACT: The precise function of C-reactive protein (CRP) as a regulator of inflammation in health and disease continues to evolve. The true understanding of its role in host defense responses has been hampered by numerous reports of comparable systems with contradictory interpretations of CRP as a stimulator, suppressor, or benign contributor to such processes. These discrepancies may be explained in part by the existence of a naturally occurring CRP isoform, termed modified CRP (i.e., mCRP), that is expressed when CRP subunits are dissociated into monomeric structures. The free mCRP subunit undergoes a non-proteolytic conformational change that has unique solubility, antigenicity, and bioactivity compared to the subunits that remain associated in the native, pentameric CRP molecule (i.e., pCRP).

SUBMITTER: Potempa LA 

PROVIDER: S-EPMC4762138 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature