Gene expression and activity of methionine converting enzymes in broiler chickens fed methionine isomers or precursors.

Poultry Science(2018)

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摘要
Common dietary supplemental methionine (Met) sources include DL-methionine (DL-Met) and the Met precursor DL-2-hydroxy-4-(methylthio) butanoic acid (DL-HMTBA). For bio-utilization, D-Met and DL-HMTBA are converted into L-Met through oxidation and transamination. The objective of this study was to determine the effect of different dietary supplemental Met sources on gene expression and enzyme activity of Met oxidases in male broiler chickens. Liver, muscle, duodenum, jejunum, and ileum were collected at days 10 (d 10), 21 (d 21), and 26 (d 26) post-hatch from male broiler chickens that were fed a basal diet deficient in sulfur amino acids (SAA) (control), or the control diet supplemented with DL-Met, L-Met, or DL-HMTBA to meet SAA requirements. The mRNA abundance of D-Met oxidase, L-HMTBA oxidase, and D-HMTBA oxidase was measured by real-time PCR, and oxidase activities were measured using colorimetric assays (n = 5). Liver expressed more D- and L-HMTBA oxidase mRNA, while breast muscle and liver expressed more D-Met oxidase mRNA than other tissues. In the liver, DL-HMTBA and L-Met supplementation were associated with greater mRNA abundance of L-HMTBA oxidase compared to the control diet-fed group at d 10 but not d 21 or d 26. DL-HMTBA supplementation, however, was not associated with changes in the mRNA abundance of D-HMTBA oxidase. The Met-deficient diet at d 26 was associated with greater hepatic abundance of DAO mRNA, which is responsible for oxidation of amino acids. Oxidase activities were similar among the Met deficient and Met-supplemented groups. In conclusion, dietary Met supplementation influenced the transcriptional regulation and activity of Met oxidases in a tissue and age-specific manner. Met oxidases may thus act as a determining factor in the bioefficacy of different dietary supplemental Met sources.
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DL-methionine,DL-2-hydroxy-4-(methylthio) butanoic acid,L-2-hydroxy acid oxidase,D-2-hydroxy acid dehydrogenase,D-amino acid oxidase
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