The first difference between glutamine and glutathione lies in the composition of these molecules. Glutamine is a conditionally essential amino acid which is a mono-peptide. Glutamine is an amide of another conditionally essential amino acid called glutamic acid. Glutamine is one of the 22 amino acids required by the body.
Glutathione is a tripeptide formed by linkage between three amino acids. The amino acids are cysteine, glycine and the monopeptide Glutamine from which Glutathione can be synthesized.
Polypeptide molecules like Glutathione are classified as proteins since it is a complete biological molecule in a stable conformation.
Mono-peptides like Glutamine are not classified as protein, as such, since they often lack a stable three dimensional structure. In fact, it is used in proteins.
In a larger sense, both glutamine and glutathione are essentially polymers (a molecule composed of repeating structural units).
However, glutamine needs to be present in the body in order to synthesize glutathione. Glutamine is also used as an anti-inflammatory in the treatment of autoimmune diseases and preserves glutathione, important for detoxification and immune support, levels in the liver. Glutamine can supply glutamate, a precursor for the synthesis of glutathione, by the hydrolysis of glutamine.
Glutathione is a tri-peptide with many roles in cells. Glutathione is produced in the human liver and plays a key role in intermediary metabolism, immune response and health. It conjugates to drugs to make them more soluble for excretion, is a co-factor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides. Glutathione, an antioxidant, protects cells from toxins such as free radicals.
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