Glutamine can participate in covalent cross-linking reactions between proteins, by forming peptide-like bonds by a transamidation reaction with lysine residues on another protein or chain. This reaction, catalyzed by clotting factor XIII, stabilizes the aggregates of fibrin formed during blood clotting. This cross-linking or aggregation reaction is catalyzed by a transamidase enzyme. Media for animal cell culture contain 10 times more glutamine than other amino acids, the excess presumably acting as a carbon source. A significant portion of the energy required to maintain cell growth of the energy produced can vary with cell type and comes from the oxidation of L-Glutamine.
Predominant Characteristics
L-Glutamine, a precursor of Glutamate, is one of the most readily available sources of energy for many rapidly dividing cell types for use in vitro. This amino acid is formed from glutamic acid by the action of glutamine synthetase. It is a clear, colorless solution at 37°C and is a key component and essential amino acid that is found in many cell-culture media formulations and in virtually all mammalian cells in culture.
A lack of L-glutamine can lead to poor cell growth and even death. When glucose levels are low and energy requirements are high, especially for rapidly proliferating cell types or cells cultured under hypoxic conditions, glutamine can be used as a primary source of energy for cells.
L-Glutamine is also suitable for molecular biology applications. Most commercially available media are formulated with L-glutamine which is either included in the basal formula or added as a supplement to the liquid formulations at the time of use. Always use an aseptic technique when handling or supplementing media after filtration.Due to the unstable nature of L-Glutamine, the dipeptide form (L-Alanyl-L-Glutamine) is a more stable form in solution and it is also autoclavable without much decomposition.
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