Site-specific modification of positively-charged surfaces on human serum albumin by malondialdehyde.

@article{Ishii2008SitespecificMO,
  title={Site-specific modification of positively-charged surfaces on human serum albumin by malondialdehyde.},
  author={Takeshi Ishii and Sohei Ito and Shigenori Kumazawa and Toyo Sakurai and Satoru Yamaguchi and Taiki Mori and Tsutomu Nakayama and Koji Uchida},
  journal={Biochemical and biophysical research communications},
  year={2008},
  volume={371 1},
  pages={28-32}
}
Malondialdehyde (MDA), a lipid peroxidation product, reacts with lysine residues in proteins. Human serum albumin (HSA) is a major target of MDA-modification of serum proteins. To identify, the modification sites of HSA by MDA in vitro, MDA-treated HSA was digested with a protease and the resulting peptides were subjected to liquid chromatography-tandem mass spectrometry. We identified six peptides, which contained a N-propenal adduct at Lys136, Lys174, Lys240, Lys281, Lys525, and Lys541, and… CONTINUE READING

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