The reactivity of human serum albumin toward trans-4-hydroxy-2-nonenal.

ABSTRACT: Mass spectrometry was used to probe the preferred locations of trans-4-hydroxy-2-nonenal (HNE) addition to the cysteine, histidine, and lysine residues of human serum albumin (HSA). Considering only those modified peptides supported by high mass accuracy Orbitrap precursor ion measurements (high confidence hits), with HNE:HSA ratios of 1:1 and 10:1, 3 and 15 addition sites, respectively, were identified. Using less stringent criteria, a total of 34 modifications were identified at the higher concentration. To gain quantitative data, iTRAQ labeling studies were completed. Previous work had identified Cys(34) , the only free cysteine, as the most reactive residue in HSA, and we have found that Lys(199) , His(242/7) , and His(288) are the next most reactive residues. Although the kinetic data

SUBMITTER: Liu Q 

PROVIDER: S-EPMC3531918 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature