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Glutamine (abbreviated as Gln or Q; encoded by the codons CAA and CAG) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain amide which replaces the side chain hydroxyl of glutamic acid with an amine functional group, classifying it as a charge neutral, polar (at physiological pH) amino acid. It is non-essential and conditionally essential in humans, meaning the body can usually synthesize sufficient amounts of it, but in some instances of stress, the body's demand for glutamine increases and glutamine must be obtained from the diet.[1][2] Nontoxic transporter of ammonia in the blood circulation.
Glutamine is one of the 20 naturally occurring amino acids in dietary protein, specifically it is a conditionally essential amino acid (being elevated to essential during periods of disease and muscle wasting typical of physical trauma). It is sold as an isolated amino acids as well as being found in high levels in dietary meats and eggs. It is found in very high levels in both Whey Protein and Casein Protein . Glutamine is a very effective intestinal and immune system health compound, as these cells use glutamine as the preferred fuel source rather than glucose.
[1] Jump up^ Dietary Reference Intakes: The Essential Guide to Nutrient Requirements, published by the Institute of Medicine's Food and Nutrition Board, currently available online at http://fnic.nal.usda.gov/dietary-guidance/dietary-reference-intakes/dri-reports
[2] Jump up^ Lacey, JM; Wilmore, DW (Aug 1990). "Is glutamine a conditionally essential amino acid?". Nutrition Reviews. 48 (8): 297–309.doi:10.1111/j.1753-4887.1990.tb02967.x.
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