title: Identification of specific oxidatively modified proteins in chicken muscles using a combined immunologic and proteomic approach.
abstract: Muscle proteins are generally believed to be key players in free radical processes that eventually lead to oxidative deterioration or modifications of meat proteins resulting in alterations in functionality, for example, gel-forming ability, emulsification properties, and water-binding capacity. This study addresses protein oxidation in chicken muscles using a combined immunologic and proteomic approach and identifies specific proteins that contain carbonyls and/or 3-nitrotyrosine (3-NT). Whereas alpha-enolase was the predominant carbonyl-reactive species among the water-soluble muscle proteins, several other proteins (actin, heat shock protein 70, and creatine kinase) contained carbonyls and/or 3-nitrotyrosine. Finally, this approach was used to demonstrate differential susceptibility of water-soluble muscle proteins toward oxidation in chickens fed a low-antioxidant diet compared with chickens fed a diet supplemented with antioxidant-rich fruits/vegetables.
authors.affiliation: Department of Food Science, Danish Institute of Agricultural Sciences, Research Centre Foulum, P.O. Box 50, DK-8830 Tjele, Denmark. jan.stagsted@agrsci.dk
authors.forename: Jan
authors.initials: J
authors.lastname: Stagsted
authors.forename: Emøke
authors.initials: E
authors.lastname: Bendixen
authors.forename: Henrik J
authors.initials: HJ
authors.lastname: Andersen
mesh_terms: D000818:Animals; D002645:Chickens; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D015151:Immunoblotting; D009124:Muscle Proteins / Q000032:analysis* / Q000737:chemistry*; D009132:Muscles / Q000737:chemistry*; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010449:Peptide Mapping; D040901:Proteomics; D012995:Solubility; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D009124:Muscle Proteins