Glutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.Glutamate-Ammonia Ligase: An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.Methionine SulfoximineDiazooxonorleucine: An amino acid that inhibits phosphate-activated glutaminase and interferes with glutamine metabolism. It is an antineoplastic antibiotic produced by an unidentified species of Streptomyces from Peruvian soil. (From Merck Index, 11th ed)Glutamates: Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.Glutamic Acid: A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Nitrogen: An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.Glutamate Synthase: An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC Isotopes: Stable nitrogen atoms that have the same atomic number as the element nitrogen, but differ in atomic weight. N-15 is a stable nitrogen isotope.Ketoglutaric Acids: A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)Glutamate Dehydrogenase: An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC An enzyme, involved in the early steps of purine nucleotide biosynthesis, that catalyzes the formation of 5-phosphoribosylamine from glutamine and phosphoribosylpyrophosphate. EC A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Nitrogenous Group Transferases: Enzymes that catalyze the transfer of nitrogenous groups, primarily amino groups, from a donor, generally an amino acid, to an acceptor, usually a 2-oxoacid. EC 2.6.Aspartic Acid: One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.Kinetics: The rate dynamics in chemical or physical systems.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing): An enzyme that catalyzes the synthesis of fructose-6-phosphate plus GLUTAMINE from GLUTAMATE plus glucosamine-6-phosphate.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Transaminases: A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.Asparagine: A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Amino Acid Transport Systems, Neutral: Amino acid transporter systems capable of transporting neutral amino acids (AMINO ACIDS, NEUTRAL).Quaternary Ammonium Compounds: Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.RNA, Transfer, Gln: A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Azaserine: Antibiotic substance produced by various Streptomyces species. It is an inhibitor of enzymatic activities that involve glutamine and is used as an antineoplastic and immunosuppressive agent.Citric Acid Cycle: A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.Anthranilate Synthase: An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. Anthranilate is the biosynthetic precursor of tryptophan and numerous secondary metabolites, including inducible plant defense compounds. EC Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.Amino Acid Transport System ASC: A ubiquitous sodium-dependent neutral amino acid transporter. The preferred substrates for this transporter system include ALANINE; SERINE; and CYSTEINE.Urea: A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Ammonium Chloride: An acidifying agent that has expectorant and diuretic effects. Also used in etching and batteries and as a flux in electroplating.Ornithine: An amino acid produced in the urea cycle by the splitting off of urea from arginine.Arginine: An essential amino acid that is physiologically active in the L-form.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Parenteral Nutrition, Total: The delivery of nutrients for assimilation and utilization by a patient whose sole source of nutrients is via solutions administered intravenously, subcutaneously, or by some other non-alimentary route. The basic components of TPN solutions are protein hydrolysates or free amino acid mixtures, monosaccharides, and electrolytes. Components are selected for their ability to reverse catabolism, promote anabolism, and build structural proteins.Enteral Nutrition: Nutritional support given via the alimentary canal or any route connected to the gastrointestinal system (i.e., the enteral route). This includes oral feeding, sip feeding, and tube feeding using nasogastric, gastrostomy, and jejunostomy tubes.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Carbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Histidine Ammonia-Lyase: An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA from HISTIDINE. Deficiency of this enzyme is associated with elevated levels of serum histidine and is called histidinemia (AMINO ACID METABOLISM, INBORN ERRORS).Citrullinebeta-Alanine: An amino acid formed in vivo by the degradation of dihydrouracil and carnosine. Since neuronal uptake and neuronal receptor sensitivity to beta-alanine have been demonstrated, the compound may be a false transmitter replacing GAMMA-AMINOBUTYRIC ACID. A rare genetic disorder, hyper-beta-alaninemia, has been reported.Amino Acid Transport System A: A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.Transglutaminases: Transglutaminases catalyze cross-linking of proteins at a GLUTAMINE in one chain with LYSINE in another chain. They include keratinocyte transglutaminase (TGM1 or TGK), tissue transglutaminase (TGM2 or TGC), plasma transglutaminase involved with coagulation (FACTOR XIII and FACTOR XIIIa), hair follicle transglutaminase, and prostate transglutaminase. Although structures differ, they share an active site (YGQCW) and strict CALCIUM dependence.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Parenteral Nutrition: The administering of nutrients for assimilation and utilization by a patient who cannot maintain adequate nutrition by enteral feeding alone. Nutrients are administered by a route other than the alimentary canal (e.g., intravenously, subcutaneously).Aminooxyacetic Acid: A compound that inhibits aminobutyrate aminotransferase activity in vivo, thereby raising the level of gamma-aminobutyric acid in tissues.PII Nitrogen Regulatory Proteins: A family of signal transducing adaptor proteins that control the METABOLISM of NITROGEN. They are primarily found in prokaryotes.Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing): An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC

Role of glutamine in human carbohydrate metabolism in kidney and other tissues. (1/3706)

Glutamine is the most abundant amino acid in the human body and is involved in more metabolic processes than any other amino acid. Until recently, the understanding of many aspects of glutamine metabolism was based on animal and in vitro data. However, recent studies using isotopic and balance techniques have greatly advanced the understanding of glutamine metabolism in humans and its role in glucose metabolism in the kidney and other tissues. There is now evidence that in postabsorptive humans, glutamine is an important glucose precursor and makes a significant contribution to the addition of new carbon to the glucose carbon pool. The importance of alanine for gluconeogenesis, viewed in terms of the addition of new carbons, is less than previously assumed. It appears that glutamine is predominantly a renal gluconeogenic substrate, whereas alanine gluconeogenesis is essentially confined to the liver. As shown recently, renal gluconeogenesis contributes 20 to 25% to whole-body glucose production. Moreover, glutamine has been shown not only to stimulate net muscle glycogen storage but also to stimulate gluconeogenesis in normal humans. Finally, in humans with type II diabetes, conversion of glutamine to glucose is increased (more so than that of alanine). The available evidence on the hormonal regulation of glutamine gluconeogenesis in kidney and liver and its alterations under pathological conditions are discussed.  (+info)

The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase. (2/3706)

The substitution of arginine for glutamine at amino acid 188 (Q188R) ablates the function of human galactose-1-phosphate uridyltransferase (GALT) and is the most common mutation causing galactosemia in the white population. GALT catalyzes two consecutive reactions. The first reaction binds UDP-glucose (UDP-Glu), displaces glucose-1-phosphate (glu-1-P), and forms the UMP-GALT intermediate. In the second reaction, galactose-1-phosphate (gal-1-P) is bound, UDP-galactose (UDP-Gal) is released, and the free enzyme is recycled. In this study, we modeled glutamine, asparagine, and a common mutation arginine at amino acid 188 on the three-dimensional model of the Escherichia coli GALT-UMP protein crystal. We found that the amide group of the glutamine side chain could provide two hydrogen bonds to the phosphoryl oxygens of UMP with lengths of 2.52 and 2.82 A. Arginine and asparagine could provide only one hydrogen bond of 2. 52 and 3.02 A, respectively. To test this model, we purified recombinant human Gln188-, Arg188-, and Asn188-GALT and analyzed the first reaction in the absence of gal-1-P by quantitating glu-1-P released using enzyme-linked methods. Gln188-GALT displaced 80 +/- 7. 0 nmol glu-1-P/mg GALT/min in the first reaction. By contrast, both Arg188- and Asn188-GALT released more glu-1-P (170 +/- 8.0 and 129 +/- 28.4 nmol/mg GALT/min, respectively). The overall, double displacement reaction was quantitated in the presence of gal-1-P. Gln188-GALT produced 80,030 +/- 5,910 nmol glu-1-P/mg GALT/min, whereas the mutant Arg188- and Asn188-GALT released only 600 +/- 71. 2 and 2960 +/- 283.6 nmole glu-1-P/mg GALT/min, respectively. We conclude from these data that glutamine at position 188 stabilizes the UMP-GALT intermediate through hydrogen bonding and enables the double displacement of both glu-1-P and UDP-Gal. The substitution of arginine or asparagine at position 188 reduces hydrogen bonding and destabilizes UMP-GALT. The unstable UMP-GALT allows single displacement of glu-1-P with release of free GALT but impairs the subsequent binding of gal-1-P and displacement of UDP-Gal.  (+info)

Kinetic impairment of nitrogen and muscle glutamine metabolisms in old glucocorticoid-treated rats. (3/3706)

Aged rats are more sensitive to injury, possibly through an impairment of nitrogen and glutamine (Gln) metabolisms mediated by glucocorticoids. We studied the metabolic kinetic response of adult and old rats during glucocorticoid treatment. The male Sprague-Dawley rats were 24 or 3 mo old. Both adult and old rats were divided into 7 groups. Groups labeled G3, G5, and G7 received, by intraperitoneal injection, 1.50 mg/kg of dexamethasone (Dex) for 3, 5, and 7 days, respectively. Groups labeled G3PF, G5PF, and G7PF were pair fed to the G3, G5, or G7 groups and were injected with an isovolumic solution of NaCl. One control group comprised healthy rats fed ad libitum. The response to aggression induced specifically by Dex (i.e., allowing for variations in pair-fed controls) appeared later in the aged rats (decrease in nitrogen balance from day 1 in adults but only from day 4 in old rats). The adult rats rapidly adapted to Dex treatment, whereas the catabolic state worsened until the end of treatment in the old rats. Gln homeostasis was not maintained in the aged rats; despite an early increase in muscular Gln synthetase activity, the Gln pool was depleted. These results suggest a kinetic impairment of both nitrogen and muscle Gln metabolisms in response to Dex with aging.  (+info)

Paraoxonase 192 Gln/Arg gene polymorphism, coronary artery disease, and myocardial infarction in type 2 diabetes. (4/3706)

Paraoxonase is an HDL-associated enzyme implicated in the pathogenesis of atherosclerosis by protecting lipoproteins against peroxidation. Its biallelic gene polymorphism at codon 192 (glutamine/arginine) has been associated with coronary artery disease (CAD). To further evaluate the role of this paraoxonase gene polymorphism for CAD in type 2 diabetes, we determined the paraoxonase genotype in 288 type 2 diabetic patients (170 with and 118 without angiographically documented CAD). The paraoxonase 192 Gln/Arg genotype was assessed using polymerase chain reaction followed by AlwI digestion. The frequency of the Gln allele was 0.656 in the CAD patients and 0.746 in the controls (chi2 = 5.36, P = 0.02). Compared with the Gln/Gln genotypes, the age-adjusted odds ratio for CAD was 1.78 (95% CI 1.08-2.96, P = 0.02) in subjects carrying at least one Arg allele. In the multivariate analysis, this association was even stronger after correction for the possible confounders age, sex, smoking history, and hypertension. Among current and former smokers, the odds ratio (OR) for having CAD among patients with at least one Arg allele was 3.58 (1.45-9.53, P < 0.01). The paraoxonase Arg allele was not associated with the history of myocardial infarction (OR 1.20 [0.73-1.99, NS]), but was with the extent of CAD (OR for three-vessel disease 1.92 [1.15-3.27, P = 0.01]). Our data indicate that the 192 Arg allele of the human paraoxonase gene is a risk factor for CAD but not myocardial infarction in type 2 diabetic patients, a risk factor further modified by cigarette smoking. This risk could possibly be explained by a reduced ability of the paraoxonase Arg isoform to protect lipoproteins against peroxidation.  (+info)

Analysis of zinc binding sites in protein crystal structures. (5/3706)

The geometrical properties of zinc binding sites in a dataset of high quality protein crystal structures deposited in the Protein Data Bank have been examined to identify important differences between zinc sites that are directly involved in catalysis and those that play a structural role. Coordination angles in the zinc primary coordination sphere are compared with ideal values for each coordination geometry, and zinc coordination distances are compared with those in small zinc complexes from the Cambridge Structural Database as a guide of expected trends. We find that distances and angles in the primary coordination sphere are in general close to the expected (or ideal) values. Deviations occur primarily for oxygen coordinating atoms and are found to be mainly due to H-bonding of the oxygen coordinating ligand to protein residues, bidentate binding arrangements, and multi-zinc sites. We find that H-bonding of oxygen containing residues (or water) to zinc bound histidines is almost universal in our dataset and defines the elec-His-Zn motif. Analysis of the stereochemistry shows that carboxyl elec-His-Zn motifs are geometrically rigid, while water elec-His-Zn motifs show the most geometrical variation. As catalytic motifs have a higher proportion of carboxyl elec atoms than structural motifs, they provide a more rigid framework for zinc binding. This is understood biologically, as a small distortion in the zinc position in an enzyme can have serious consequences on the enzymatic reaction. We also analyze the sequence pattern of the zinc ligands and residues that provide elecs, and identify conserved hydrophobic residues in the endopeptidases that also appear to contribute to stabilizing the catalytic zinc site. A zinc binding template in protein crystal structures is derived from these observations.  (+info)

Deamidation of alpha-A crystallin from nuclei of cataractous and normal human lenses. (6/3706)

PURPOSE: To quantitate the extent of deamidation of asparagine-101, glutamine-50, and glutamine-6 of alpha-A crystallin in the nucleus from human cataractous and normal lenses. METHODS: Reverse phase chromatography was used to prepare alpha-A crystallin from total proteins of the nucleus from cataractous and age-matched normal human lenses. Synthetic peptides were made corresponding to the expected amidated and deamidated tryptic fragments containing asparagine-101, glutamine-50, and glutamine-6. The peptides were used to identify and quantitate amidated and deamidated forms of tryptic fragments from alpha-A crystallin eluting from a reverse phase column. RESULTS: Significant amounts of deamidation of asparagine-101 and glutamine-50, but not glutamine-6, were present in alpha-A crystallin from nuclear sections of both cataractous and age-matched normal lenses. Quantitative analysis of tryptic peptides containing these residues indicated no statistical difference in deamidation in cataractous versus normal lenses. CONCLUSIONS: There was no significant difference in the extent of deamidation of asparagine-101, glutamine-50, and glutamine-6 for alpha-A crystallin, purified from the nucleus of cataractous versus age-matched normal lenses. These results strongly suggest that deamidation of these residues does not play a role in the biogenesis of human nuclear cataract.  (+info)

Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor. (7/3706)

Peptide toxins selective for particular subunit interfaces of the nicotinic acetylcholine receptor have proven invaluable in assigning candidate residues located in the two binding sites and for determining probable orientations of the bound peptide. We report here on a short alpha-neurotoxin from Naja mossambica mossambica (NmmI) that, similar to other alpha-neurotoxins, binds with high affinity to alphagamma and alphadelta subunit interfaces (KD approximately 100 pM) but binds with markedly reduced affinity to the alphaepsilon interface (KD approximately 100 nM). By constructing chimeras composed of portions of the gamma and epsilon subunits and coexpressing them with wild type alpha, beta, and delta subunits in HEK 293 cells, we identify a region of the subunit sequence responsible for the difference in affinity. Within this region, gammaPro-175 and gammaGlu-176 confer high affinity, whereas Thr and Ala, found at homologous positions in epsilon, confer low affinity. To identify an interaction between gammaGlu-176 and residues in NmmI, we have examined cationic residues in the central loop of the toxin and measured binding of mutant toxin-receptor combinations. The data show strong pairwise interactions or coupling between gammaGlu-176 and Lys-27 of NmmI and progressively weaker interactions with Arg-33 and Arg-36 in loop II of this three-loop toxin. Thus, loop II of NmmI, and in particular the face of this loop closest to loop III, appears to come into close apposition with Glu-176 of the gamma subunit surface of the binding site interface.  (+info)

Solution structure of the alpha-subunit of human chorionic gonadotropin. (8/3706)

The three-dimensional solution structure of the alpha-subunit in the alpha, beta heterodimeric human chorionic gonadotropin (hCG), deglycosylated with endo-beta-N-acetylglucosaminidase-B (dg-alpha hCG), was determined using 2D homonuclear and 2D heteronuclear 1H, 13C NMR spectroscopy at natural abundance in conjunction with the program package XPLOR. The distance geometry/simulated annealing protocol was modified to allow for the efficient modelling of the cystine knot motif present in alpha hCG. The protein structure was modelled with 620 interproton distance restraints and the GlcNAc residue linked to Asn78 was modelled with 30 protein-carbohydrate and 3 intraresidual NOEs. The solution structure of dg-alpha hCG is represented by an ensemble of 27 structures. In comparison to the crystal structure of the dimer, the solution structure of free dg-alpha hCG exhibits: (a) an increased structural disorder (residues 33-57); (b) a different backbone conformation near Val76 and Glu77; and (c) a larger flexibility. These differences are caused by the absence of the interactions with the beta-subunit. Consequently, in free dg-alpha hCG, compared to the intact dimer, the two hairpin loops 20-23 and 70-74 are arranged differently with respect to each other. The beta-GlcNAc(78) is tightly associated with the hydrophobic protein-core in between the beta-hairpins. This conclusion is based on the NOEs from the axial H1, H3, H5 atoms and the N-acetyl protons of beta-GlcNAc(78) to the protein-core. The hydrophobic protein-core between the beta-hairpins is thereby shielded from the solvent.  (+info)

  • Our Glutamine 1000 Caps are formulated for rapid disintegration and provide 1,000 mg of pure L-Glutamine per capsule so they deliver a quick, powerful dose each and every time. (
  • If glucose is your body's favorite fuel (and it is), then glutamine is your body's favorite amino acid, or very nearly so. (
  • Thus, by adding glutamine to your post-workout protein shake instead of carbohydrate, for instance, you effectively replenish your body's glucose economy, but in a way that actually stimulates the burning of fat as opposed to reducing it (i.e., as eating carbohydrate normally tends to do). (
  • Intense exercise can quickly deplete glutamine in the muscle cells causing the immune system to weaken and decreases the body's levels of glutamine. (
  • It has been proven that glutamine plays an important role in the body's natural defences. (
  • High levels of cortisol can lower your body's stores of glutamine. (
  • And the body's ability to expel glutamine means that many doctors see glutamine as benign, with no side effects even at high doses. (
  • Ingredients: L-Glutamine. (
  • Allmax Glutamine is manufactured with the purest raw ingredients at a Pharmaceutical Grade Manufacturing facility ALLMAX Nutrition™ Japanese Micronized Glutamine provides recovery after training and enhances the immune system that can be compromised during intense exercise. (
  • Trade Ingredients purchase Glutamine in large volumes direct from the manufacturer. (
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  • Taking a combination product containing glutamine and other ingredients doesn't seem to improve the healing rate of foot sores in glutamine with diabetes. (
  • Taking a combination of glutamine and other ingredients might reduce the mood-related ffacts associated with opioid withdrawal. (
  • If however, the body is subjected to major stress such as intense exercise , illness or injury, your glutamine requirements exceed the ability of your body to produce sufficient amounts. (
  • After an intense workout, glutamine levels are greatly depleted in your body, which decreases strength, muscle growth and recovery. (
  • Supplementing with CNP Professional's Pro-Glutamine could help assist with the catabolic action of cortisol (breakdown of muscle) created by intense exercise. (
  • Much of this glutamine is inefficiently used and secreted from the cells as lactic acid, ammonia, or alanine, a situation with many parallels to the inefficient metabolism of glucose by many cancer cells (1). (
  • Glutamine is important for removing excess ammonia (a common waste product in the body). (
  • Hagen and her co-authors had previously shown that glutamine protects against cell death from H. pylori-produced ammonia. (
  • Our work demonstrated that the damaging effects of ammonia on gastric cells could be reversed completely by the administration of L-glutamine," explains Hagen. (
  • Glutamine also helps the body to recover from ammonia toxicity. (
  • L-Glutamine also helps in buffering poisonous wastes in the body such as ammonia. (
  • Supplemental glutamine is often given to malnourished cancer patients undergoing chemotherapy or radiation treatments, and sometimes used in people undergoing bone marrow transplants. (
  • To test this hypothesis, the investigators divided 105 mice into two groups, which were fed either a standardized diet (containing 1.9 percent glutamine) or the same diet with supplemental L-glutamine (containing 6.9 percent glutamine) replacing carbohydrates for five percent of the total calories. (
  • Those in group P received the continuous infusion of parenteral glutamine dipeptide supplement (Dipeptiven 100ml, Fresenius Kabi) and were fed enterally with a standard commercial enteral polymeric diet without added glutamine (Ensure, Abbott Ross). (
  • TORC1 seemed to respond to glutamine as well as essential amino acid levels. (
  • Glutamine is a semi essential amino acid that the body produces in small amounts. (
  • As L-Glutamine is only considered as a semi-essential amino acid, this means that the body will be able to generate its own supply of glutamine that it needs. (
  • Glutamine Plus also features Sustamine, a unique dipeptide ingredient that combines the amino acids L-Alanine and L-Glutamine to help your body rehydrate, replenish and recover. (
  • Glutamine, a nonessential amino acid, is preferred fuel for rapidly proliferating cells in human body. (
  • Glutamine is a nonessential amino acid naturally found in certain foods, including beef, chicken, fish, eggs, dairy products and some fruits and vegetables. (
  • In addition, glutamine was suggested to improve gut immune function [ 10 , 11 ]. (
  • An early study shows that giving glutamine glutamine by Allergy along with intravenous nutrition improves immune function but does not reduce the risk for complications gltamine the amount of time spent in the hospital in people with pancreatitis. (
  • Because your white blood cells rely on muscle glutamine for reproduction, your beloved biceps actually figure as an important part of your immune system, something you might not think about while exercising. (
  • But in the absence of a chronic shortage, glutamine does not seem to enhance performance or muscle growth. (
  • Exercise (especially resistance training) and hormones (especially testosterone and growth hormone) assists the processes and there are specific amino acids like glutamine and the BCAA group (especially leucine) which really augment and increase the muscle acquisition processes. (
  • Glutamine can be of value for higher-protein/lower-carbohydrate eaters such as myself by serving as a 'non-carbohydrate' means of re-fueling your body (e.g., liver and muscle glycogen replenishment), with a fat-burning 'kick' to boot (i.e., stimulation of gluconeogenesis and associated increased oxidation of fatty acids). (
  • Additionally, one of the inner signals to stimulate growth or to cause a mechanical signal to the muscle to result in biochemical growth is the influx-efflux of glutamine in and out of the muscle cell. (
  • It seems to build muscle that your body draws glutamine from varying body sites and Dr. Connelly postulated that using glutamine in substrate cycling, (providing constant glutamine to the system would result in constant signals to build more muscle without robbing glutamine from the gut and it appears he was right and way ahead of the game (I mean way ahead). (
  • Glutamine does provide notable benefits for muscle growth, but it does have other health advantages which may not be so widely known. (
  • Glutamine helps by preserving muscle mass and preventing catabolic effects. (
  • Studies have shown that L-glutamine supplementation can improve protein metabolism, increase recovery, minimize muscle breakdown and boost your stamina. (
  • Glutamine is one of the most important amino acids and is required by every muscle in the human body. (
  • Anyone involved in high intensity training programmes will find Glutamine a beneficial supplement, especially with muscle tissue being the primary source of glutamine in the blood. (
  • During critical illness, trauma, intestinal disease, starvation,(intravenous feeding), wasting (excessive loss of lean body mass), and extreme endurance exercise and to preserve muscle mass when dieting, Glutamine was shown to be beneficial. (
  • L-glutamine - the biologically active isomer of glutamine - is widely used as a dietary supplement by body builders to increase muscle mass. (
  • Glutamine Reduces Muscle Deterioration: Glutamine is high in demand throughout the body and is used in the gut and immune system extensively to maintain optimal performance. (
  • Studies show that training over an extended period of time, rapidly depletes both muscle and blood glutamine levels. (
  • What's worse, during periods of stress, glutamine is further depleted, and if not reversed, glutamine is pulled directly from the muscle. (
  • When supplemented, it may help body builders reduce the amount of muscle deterioration that occurs because other tissues that need glutamine will not rob the glutamine stored in the muscle. (
  • There is some evidence that glutamine might help to reduce muscle and joint pains allregy allergy paclitaxel. (
  • These include: Hormone production Neurotransmitter production Muscle growth Immune system function Anti-inflammatory properties Gut health improvement All of the processes that glutamine is involved in are necessary for running a healthy body. (
  • Lower glutamine-levels were also associated with larger fat cell size and higher body fat percentage independently of body-mass index (BMI), according to the study. (
  • This means that a lack of glutamine, which may occur during long-term obesity, could lead to epigenetic changes that fuel inflammation in the body. (
  • Glutamine is the main mitochondrial substrate that is required to maintain the membrane potential in mitochondria of cancer cells as well as aid in NADPH production that is necessary for synthesizing other macromolecules as well as control redox chemical reactions within the body. (
  • When you take glutamine, you provide your body with one of the most important fuels it needs. (
  • At this point your body may need more Glutamine than it can produce making supplementation advantageous. (
  • Glutamine supplementation may support the removal of waste products in the body, digestion and immune system function. (
  • Stress on the body can also result in inadequate amounts of Alanine, which along with Glutamine, is considered to be the most one of the important of the amino acids for actual amino acid metabolism. (
  • Reason being, the more intensely you work your body and the more stress you put yourself through, the more your body will use glutamine. (
  • The body can make enough glutamine for its regular needs. (
  • But during times of extreme stress (the kind you experience after heavy exercise or an injury), your body may need more glutamine than it can make. (
  • You can usually get enough glutamine without taking a supplement because your body makes it and you get some in your diet. (
  • It is a common belief that L-Glutamine is only useful as a health supplement glutamine those involved in extreme physical activities, such as body builders and weight lifters. (
  • L-Glutamine plays an important role in controlling and maintaining allergy amino acid balance in the human body when it is subjected to severe stress levels. (
  • The human body synthesizes more amount of glutamine which is further involved in numerous biochemical process of life. (
  • Tangentially, glutamine is also recommended by some to abate sugar cravings, or among body builders and athletes for performance and recovery. (
  • Glutamine has many functions in the body. (
  • Glutamine might help gut function, the immune system, and other essential processes in the body, especially in times of stress. (
  • We know, however, that glutamine is also important for cell division and the metabolism of cancer and therefore, more research on possible long-term side effects is needed before glutamine may be recommended as a dietary supplement to help treat obesity and its complications. (
  • Glutamine is a good choice for anyone participating in a physical training, getting the correct dietary balance is absolutely essential. (
  • The first step was to establish and validate a bolus injection method to measure glutamine endogenous rate of appearance (endoRa) for studying endogenous glutamine production in the ICU setting. (
  • Because many of the stomach pathologies during H. pylori infection [including cancer progression] are linked to high levels of inflammation, this result provides us with preliminary evidence that glutamine supplementation may be an alternative therapy for reducing the severity of infection," explains Hagen, adding that studies in human subjects will be the next step to determine the relevance of this finding in the clinical setting. (
  • Glutamine could help people with obesity reduce inflammation of fat tissue and reduce fat mass, according to a new study at Karolinska Institutet in Sweden and the University of Oxford in the U.K. The researchers also show how glutamine levels can alter gene expression in several different cell types. (
  • People with obesity had on average lower levels of glutamine in their fat tissue than normal-weight people. (
  • The researchers also showed through a combination of animal and cell analyses that glutamine levels influenced the expression of different genes and that low glutamine levels induced an increase in the expression of pro-inflammatory genes in the fat tissue. (
  • The researchers also studied in detail what happens inside the fat cell when glutamine levels are altered. (
  • People with obesity had higher levels of O-GlcNAcylation in their fat tissue while mice and human cells treated with glutamine had lower levels of O-GlcNAcylation in the cell nucleus. (
  • as well as gender- and diagnosis-related differences in glutamine levels were also investigated. (
  • 930 μmol/L). No significant difference could be detected between glutamine levels and gender or diagnosis categories as a group. (
  • A CRP cut-off value of 95.5 mg/L was determined above which glutamine levels became deficient. (
  • About a third of patients (38 %) were glutamine deficient on admission to ICU, whereas some presented with supra-normal levels. (
  • While glutamine levels correlated inversely with inflammatory markers, and a CRP value of above 95.5 mg/L indicated potential glutamine deficiency, the clinical application of this finding needs further investigation. (
  • Many people with cancer have low levels of glutamine. (
  • It could take up to one week for glutamine levels to return to normal. (
  • Some researchers think it works best in people with low glutamine levels during chemotherapy treatment. (
  • Exercising at 90 to 120 percent of maximal oxygen uptake can bring about a significant, though transient, drop in blood glutamine. (
  • From studying how glutamine is taken up through an importer called SLC1A5 showed that glutamine was exported using SLC7A5 which exchanges glutamine for uptake of essential amino acids. (