Proteomics of lipid oxidation-induced oxidation of porcine and bovine oxymyoglobins.

@article{Suman2007ProteomicsOL,
  title={Proteomics of lipid oxidation-induced oxidation of porcine and bovine oxymyoglobins.},
  author={Surendranath P. Suman and Cameron Faustman and Sheryl L Stamer and Daniel C. Liebler},
  journal={Proteomics},
  year={2007},
  volume={7 4},
  pages={628-640}
}
Myoglobin (Mb) redox state affects meat color and is destabilized by lipid oxidation products such as 4-hydroxy-2-nonenal (HNE). Our objective was to investigate lipid oxidation-induced oxymyoglobin (OxyMb) oxidation in Mb from two major meat-producing livestock species utilizing MS and proteomics tools. Porcine OxyMb was incubated with HNE and analyzed for metmyoglobin (MetMb) formation. MetMb formation was greater in the presence of HNE than controls at pH 7.4 and 37 degrees C (p <0.05… CONTINUE READING