Results 251 to 260 of about 538,260 (299)
The Effect of Glutamine Administration on Intestinal Glutamine Content
Journal of Surgical Research, 1996 The small intestine has been identified as an important site of metabolism of glutamine. The impairment of gut mucosa integrity during total parenteral nutrition (TPN) has been ascribed to a diminished supply of glutamine, due to the lack of glutamine in standard TPN. In addition, nutritional depletion diminishes glutamine availability in the intestine.
van der Hulst, R.R.W.J. +4 more
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The importance of cytosolic glutamine synthetase in nitrogen assimilation and recycling [PDF]
New Phytologist, 2009 Glutamine synthetase assimilates ammonium into amino acids, thus it is a key enzyme for nitrogen metabolism. The cytosolic isoenzymes of glutamine synthetase assimilate ammonium derived from primary nitrogen uptake and from various internal nitrogen ...
Dimah Habash
exaly +2 more sources
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2012
Glutamine (GLN) has been shown to be a key pharmaconutrient in the body's response to stress and injury. It exerts its protective effects via multiple mechanisms, including direct protection of cells and tissue from injury, attenuation inflammation, and preservation of metabolic function.
Mike, Kim, Paul E, Wischmeyer
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Glutamine (GLN) has been shown to be a key pharmaconutrient in the body's response to stress and injury. It exerts its protective effects via multiple mechanisms, including direct protection of cells and tissue from injury, attenuation inflammation, and preservation of metabolic function.
Mike, Kim, Paul E, Wischmeyer
+6 more sources
Role of glutamine synthetase in angiogenesis beyond glutamine synthesis [PDF]
Nature, 2018 Glutamine synthetase, encoded by the gene GLUL, is an enzyme that converts glutamate and ammonia to glutamine. It is expressed by endothelial cells, but surprisingly shows negligible glutamine-synthesizing activity in these cells at physiological ...
Charlotte Dubois +2 more
exaly +3 more sources
World Journal of Surgery, 2000
AbstractRelatively little was known about glutamine metabolism until the 1930s, when Sir Hans Krebs first demonstrated glutamine hydrolysis and biosynthesis in the kidney. Subsequent studies by Rose in 1938 demonstrated that glutamine is a nonessential (dispensable) amino acid, as it can be readily synthesized de novo in virtually all tissues in the ...
B I, Labow, W W, Souba
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AbstractRelatively little was known about glutamine metabolism until the 1930s, when Sir Hans Krebs first demonstrated glutamine hydrolysis and biosynthesis in the kidney. Subsequent studies by Rose in 1938 demonstrated that glutamine is a nonessential (dispensable) amino acid, as it can be readily synthesized de novo in virtually all tissues in the ...
B I, Labow, W W, Souba
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The synthesis of glutamine and asparagine peptides and of glutamine
Archives of Biochemistry and Biophysics, 1952Summary A new synthesis of glutaminylglycine and the synthesis of a new peptide, asparaginylglycine, are reported. The syntheses of glycylglutamine, glycylasparagine, and glutamine have been reinvestigated. A method for the purification of commercial glutamine is proposed.
H K, MILLER, H, WAELSCH
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Congenital Glutamine Deficiency with Glutamine Synthetase Mutations
New England Journal of Medicine, 2005Glutamine synthetase plays a major role in ammonia detoxification, interorgan nitrogen flux, acid-base homeostasis, and cell signaling. We report on two unrelated newborns who had congenital human glutamine synthetase deficiency with severe brain malformations resulting in multiorgan failure and neonatal death.
Johannes, Häberle +11 more
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Amino Acids, 2017
The synthetic dipeptides alanyl-glutamine (Ala-Gln) and glycyl-glutamine (Gly-Gln) are used as Gln substitution to provide energy source in the gastrointestinal tract due to their high solubility and stability. This study aimed to investigate the effects of Gln, Ala-Gln and Gly-Gln on mitochondrial respiration and protein turnover of enterocytes ...
Bie Tan +8 more
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The synthetic dipeptides alanyl-glutamine (Ala-Gln) and glycyl-glutamine (Gly-Gln) are used as Gln substitution to provide energy source in the gastrointestinal tract due to their high solubility and stability. This study aimed to investigate the effects of Gln, Ala-Gln and Gly-Gln on mitochondrial respiration and protein turnover of enterocytes ...
Bie Tan +8 more
openaire +2 more sources
Nutrition, 2000
The goal of the present work was to compare the plasma glutamine response to exogenous glutamine administration in human volunteers; glutamine was provided as a free amino acid, bound to proteins, or in the form of peptides. Plasma glutamine concentrations were measured in eight human volunteers at 30, 60, 90, 120, and 240 min after receiving a drink ...
J J, Boza +3 more
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The goal of the present work was to compare the plasma glutamine response to exogenous glutamine administration in human volunteers; glutamine was provided as a free amino acid, bound to proteins, or in the form of peptides. Plasma glutamine concentrations were measured in eight human volunteers at 30, 60, 90, 120, and 240 min after receiving a drink ...
J J, Boza +3 more
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, 2008 Inelastic Neutron Scattering spectrum of Glutamine, C₅H₁₃N₂O₄, measured on the TFXA ...
P. Haris, De Montfort University
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