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ABSTRACT: Objective
This study aimed to investigate how growth-related myopathies influenced chemical modifications formed on amino acid residues of chicken breast proteins.Methods
Breasts (pectoralis major) of commercial broilers (Gallus gallus) were classified into "normal", White Striping (WS)" and "White Striping + Wooden Breast (WS+WB)" groups (n = 9 per group). The meat was subjected to proteomic analysis using a liquid chromatography-tandem mass spectrometry. Differences in abundance of modified sites, including methylated lysine (Lys) and arginine, acetsylated Lys, and oxidized methionine (Met), due to the growth-related myopathies were identified (false discovery rate [FDR]<0.05). Biological functions of the proteins were analyzed.Results
Proteomics revealed 185, 105
SUBMITTER: Malila Y
PROVIDER: S-EPMC12415449 | biostudies-literature | 2025 Sep
REPOSITORIES: biostudies-literature