Site-specific arylation of rat glutathione s-transferase A1 and A2 by bromobenzene metabolites in vivo.

ABSTRACT: The hepatotoxicity of bromobenzene (BB) derives from its reactive metabolites (epoxides and quinones), which arylate cellular proteins. Application of proteomic methods to liver proteins from rats treated with a hepatotoxic dose of [14C]-BB has identified more than 40 target proteins, but no adducted peptides have yet been observed. Because such proteins are known to contain bromophenyl- and bromodihydroxyphenyl derivatives of cysteine, histidine, and lysine, the failure to observe modified peptides has been attributed to the low level of total covalent binding and to the "dilution" effect of multiple metabolites reacting at multiple sites on multiple proteins. In this work glutathione S-transferase (GST), a well-known and abundant BB-target protein, was isolated from liver cytosol of rats

SUBMITTER: Koen YM 

PROVIDER: S-EPMC1661840 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature