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Proteomic Study of Differential Proteins in Different Muscles from White Feathered Broilers Based on Sequential Window Acquisition of All Theoretical Fragment-Ion Spectra |
LIU Zhihong, NAI Rile, XIE Yuchun, MI Lu, MA Lina, ZHAO Meng, SUN Ang, LI Jinquan, WANG Zhixin |
1.Engineering Research Center for Goat Genetics and Breeding, Inner Mongolia Autonomous Region, Key Laboratory of Mutton Sheep Genetics and Breeding, Ministry of Agriculture, Key Laboratory of Animal Genetics, Breeding and Reproduction, Inner Mongolia Autonomous Region, College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China; 2.Inner Mongolia Academy of Agricultural and Animal Husbandry Sciences, Hohhot 010018, China; 3.College of Economics and Management, Inner Mongolia Agricultural University, Hohhot 010018, China |
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Abstract Protein is a major food component and its changes lead to changes in meat quality. Muscles from different carcass parts vary in terms of physicochemical properties and protein composition. In this study, protein identification and quantitative analysis of white feathered broilers breast and thigh muscles were carried out by data independent acquisition (DIA) and sequential window acquisition of all theoretical fragment-ion spectra (SWATH) techniques, and bioinformatics analysis was performed as well. The results showed that a total of 875 proteins and 16 855 peptide fragments were detected in thigh and breast meat. Out of these, 98 differentially expressed proteins were screened. Gene ontology (GO) enrichment analysis evidenced that the 71 up-regulated proteins found in chicken were involved in biological processes (BP) such as fatty acid beta-oxidation using acylcoenzyme A (CoA) dehydrogenase, the tricarboxylic acid cycle and lipid homeostasis; in terms of cell components, they were mainly concentrated in mitochondria; their molecular functions (MF) included participating in reductase activity, fatty acyl CoA binding, nicotinamide adenine dinucleotide (NAD) binding, movement, electron carrier activity, flavin adenine dinucleotide binding and catalytic activity. The 27 up-regulated proteins in chicken breast were the most abundant in the process of skeletal muscle contraction and cardiac muscle contraction; they were enriched in the extracellular exosome, and none of the proteins was enriched in MF. The highly expressed proteins in chicken thigh meat were enriched in movement-related functions, while those in chicken breast meat were enriched in muscular contraction.
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