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

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 t...

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Veröffentlicht in:	Proteomics (Weinheim) 2007-02, Vol.7 (4), p.628-640
Hauptverfasser:	Suman, Surendranath P., Faustman, Cameron, Stamer, Sheryl L., Liebler, Daniel C.
Format:	Artikel
Sprache:	eng
Schlagworte:	4-Hydroxy-2-nonenal Aldehydes - chemistry Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Fundamental and applied biological sciences. Psychology Histidine - chemistry Hydrogen-Ion Concentration Lipid oxidation Lipids - chemistry Mass Spectrometry Miscellaneous Models, Molecular Molecular Sequence Data Myoglobin Myoglobin - chemistry Myoglobin - metabolism Oxidation-Reduction Peptides - analysis Proteins Proteome - metabolism Swine Temperature
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Beschreibung
Zusammenfassung:	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°C (p
ISSN:	1615-9853 1615-9861
DOI:	10.1002/pmic.200600313