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Discover Supplement-Drug Interactions
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Last Updated: 3 years ago
supplement:
Arginine
supplement:
Glutamic Acid
Research Papers that Mention the Interaction
“At 1 h post feeding, L-Arg mares had lower (P<0.05) plasma concentrations of histidine, glutamic acid , proline, isoleucine, threonine, phenylalanine, leucine, valine, alanine, and taurine.”
Orally supplemented L-arginine impairs amino acid absorption depending on dose in horses.“The results showed that dietary supplementation with arginine, glutamic acid, or … 5'-nucleotides and meat sensory taste traits, but supplementation with arginine … glutamic acid significantly increased (P < 0.05) fat accumulation and fatty acid content in muscle, … compounds, and improved the tenderness, juiciness, and overall eating quality of meat.”
Fatty Acid Content, Flavor Compounds, and Sensory Quality of Pork Loin as Affected by Dietary Supplementation with l-arginine and Glutamic Acid.“The level of arginine decreased by 13% and glutamic acid by 39%.”
“Collectively, these findings suggest that dietary supplementation with both Arg and Glu increases intramuscular FAA concentrations and decreases the mRNA levels of genes involved in protein degradation in skeletal muscle.”
“We found that l-Arg significantly improved the physical stability of spray-dried BSA even at low concentrations, however, when combined with l-Glu , was ineffective at reducing monomer BSA loss.”
“l‐Glutamine (0.2 mm and 2 mm) but not d‐glutamine (2 mm), l‐glutamic acid (2 mm) or ammonium chloride (1 mm) also inhibited the generation of l‐arginine in endothelial cells.”
“ Arginine and its analog, canavanine, inhibited to the same degree TPA-induced ornithine decarboxylase activity, and potentiated to the same extent the inhibitory effects of glutamic acid , asparagine, and glycine on this enzyme.”
“Salt bridge formation between glutamic acid at position 86 and arginine at position 120 in the neighboring chain may be responsible for the slight shift of the chain fragment, thus creating wider access to the active site both for the substrate and PLP.”
Improving thermal stability of thermophilic L-threonine aldolase from Thermotoga maritima.“Substitution of a single arginine with a glutamic acid residue in the loop connecting the two TM domains at the cell surface greatly improves its function.”
“These results suggest that the conserved arginine residue in GH10 xylanases increases the pK a value of the proton donor Glu during substrate binding.”
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