Protein-selective capture to analyze electrophile adduction of hsp90 by 4-hydroxynonenal.
作者： Rebecca E. Connor , Lawrence J. Marnett , Daniel C. Liebler
DOI: 10.1021/TX200157T
关键词:
摘要: The analysis of protein modification by electrophiles is a challenging problem. Most reported protein–electrophile adducts have been characterized from in vitro reactions or through affinity capture the adduct moiety, which enables global analyses but poorly suited to targeted studies specific proteins. We employed molecular probe approach study modifications chaperone heat shock 90 (Hsp90), regulates diverse client Noncovalent with biotinyl–geldanamycin isolated both isoforms native (Hsp90α and Hsp90β) human RKO colorectal cancer cells. Geldanamycin–biotin afforded higher purity Hsp90 than did immunoprecipitation enabled detection endogenously phosphorylated liquid chromatography–tandem mass spectrometry (LC-MS/MS). applied this map quantify formed on 4-hydroxynonenal (HNE) LC-MS/MS tryptic digests identifie...
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