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  1. #1
    Slugger is offline Junior Member
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    Glutamine with water

    Is it ok to mix glutamine with water or is it best to mix it with something like gatorade?

    Right now I'm mixing with water 10 g post workout and 10 g before bed.

  2. #2
    RP7's Avatar
    RP7
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    You dont need a sugar (like dextrose) to spike your insulin for glutamine. Just take it on an empty stomach so you can get good absorption. If you want to mix it, go nuts.

  3. #3
    Brazy is offline Junior Member
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    i've been told taking glutamine on an empty stomach goes towards restoring glycogen..

    i've been told its best to take it 15 min after a meal.. and thats what i've done and it seems to does it part well

    and i mix 5g with a glass of water

  4. #4
    Blackac is offline Associate Member
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    So whats the rule of thumb with glutamine, 3000mg before the work out and 3000mg after workout....and on an empty stomach......i have capsules..

  5. #5
    Elliot's Avatar
    Elliot is offline Anabolic Member
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    caps are horrible its a total rip off.. get protein powder that already has it.. www.allthewhey.com for example..

  6. #6
    Valmont is offline Banned
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    Glutamine peptides. preferbly on empty stomach after morning cardio.

    Ice is a pretty good supplement as well. or you could check with macphage on here, he will hook you up.

  7. #7
    baller45's Avatar
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    I have a different opinion about oral glutamine, since the small intestine uses it all for energy.

    "Oral is useless for what most want it to do. Take a dipeptide if you want to see it work. "-Animal

  8. #8
    K-pac is offline New Member
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    slugger,

    I don't think that you need to take 20g of glutamine a day. I think 5-10g post workout should suffice. Correct me if I am wrong guys.
    K-pac

  9. #9
    daman1's Avatar
    daman1 is offline Diet Specialist
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    Quote Originally Posted by K-pac
    slugger,

    I don't think that you need to take 20g of glutamine a day. I think 5-10g post workout should suffice. Correct me if I am wrong guys.
    K-pac
    You are correct. I would take 5g's p.w. and 5g's before bedtime.

  10. #10
    baller45's Avatar
    baller45 is offline Junior Member
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    No. If you take whey you are getting enough already. I can't stand peole wasting money. Can anyone actually tell me that extra free-form glutamine does anthing but get sucked up by the small intestine? No, you can't.

  11. #11
    RP7's Avatar
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    Quote Originally Posted by baller45
    No. If you take whey you are getting enough already. I can't stand peole wasting money. Can anyone actually tell me that extra free-form glutamine does anthing but get sucked up by the small intestine? No, you can't.
    Then don't take it. Let us all waste our money in peace. And why don't you enlighten us with your knowledge since we cant prove anything.

  12. #12
    baller45's Avatar
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    Quote Originally Posted by RP7
    Then don't take it. Let us all waste our money in peace. And why don't you enlighten us with your knowledge since we cant prove anything.
    Hehe!
    Here...

  13. #13
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    The entire piece was written because of free form glutamine's lack of effectiveness.

    New Developments in Glutamine Delivery1
    Peter Fürst2

    University of Hohenheim, Institute for Biological Chemistry and Nutrition, Stuttgart, Germany



    2To whom correspondence should be addressed. E-mail: b-c-nutr@uni-hohenheim.de




    ABSTRACT
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    ABSTRACT
    INTRODUCTION
    Dipeptide concept
    Glutamine dipeptides: a new...
    Implications for glutamine...
    Alternative nitrogen-containing...
    LITERATURE CITED


    Numerous studies demonstrate that free glutamine can be added to commercially available crystalline amino acid-based preparations before their administration. Instability during heat sterilization and prolonged storage and limited solubility (35 g/L at 20°C) hamper the use of free glutamine in the routine clinical setting. Indeed, there are many well-controlled and valuable trials with free glutamine, yet its use is restricted to clinical research. The obvious limitations of using free glutamine initiated an intensive search for alternative substrates. Synthetic glutamine dipeptides are stable under heat sterilization and highly soluble; these properties qualify the dipeptides as suitable constituents of nutritional preparations. Industrial production of these dipeptides at a reasonable price is an essential prerequisite for implications of dipeptide-containing solutions in clinical practice. Recent development of novel synthesis procedures allows increased capacity in industrial-scale production. Basic studies with synthetic glutamine-containing short-chain peptides provide convincing evidence that these new substrates are cleared rapidly from plasma after parenteral administration, without being accumulated in tissues and with negligible loss in urine. The presence of membrane-bound as well as tissue-free extracellular hydrolase activity facilitates a prompt and quantitative peptide hydrolysis, the liberated amino acids being available for protein synthesis and/or generation of energy. In the clinical setting, glutamine dipeptide nutrition beneficially influences outcome (nitrogen balance, immunity, gut integrity, hospital stay, morbidity and mortality). The provision of conditionally indispensable glutamine should be considered a necessary replacement of a deficiency rather than a supplementation. The beneficial effects observed with glutamine dipeptide nutrition should be seen simply as a correction of disadvantages produced by the inadequacy of conventional clinical nutrition. The availability of stable dipeptide preparations certainly facilitates, for the first time, adequate amino acid nutrition of critically ill, malnourished or stressed patients in the routine clinical setting and, thus, represents a new dimension in artificial nutrition.


    Key Words: glutamine dipeptides • ornithine -ketoglutarate • acetylated amino acids • short chain protein hydrolysates • catabolic stress


    INTRODUCTION
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    INTRODUCTION
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    Glutamine dipeptides: a new...
    Implications for glutamine...
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    Available data strongly support the notion that glutamine should be an essential part of parenteral nutrition in various diseased states (Wilmore and Shabert 1998 , Fürst et al. 2000a, Griffiths 1999 ). However, two unfavorable physical chemical properties prevent the inclusion of free glutamine in commercially available amino acid preparations; the quantitative decomposition of aqueous glutamine to the cyclic product associated with ammonia liberation (Fürst et al. 1990 ) and its limited solubility in water (35 g/L H2O at 20°C). Therefore, glutamine-containing TPN solutions must be prepared freshly under strict aseptic conditions and stored at 4°C. To diminish the risk of precipitation, the glutamine concentration in such solution should not exceed 2.5%. This means that provision of adequate amounts of glutamine to injured or critically ill patients represents a severe burden, especially in volume-restricted situations. Consequently, parenteral use of free glutamine is reserved for controlled clinical trials and only in countries allowing nonheat-sterilized solutions.

    Controlled clinical studies with free glutamine showed improved nitrogen balance and rate of protein synthesis (Griffiths 1999 , Hammarqvist et al. 1989 , Ziegler et al. 1992 , Li et al. 1997 ) compared with control groups. Post-bone marrow transplantation morbidity was reduced with supplemental glutamine; the incidence of clinical infection, total and site-specific microbial colonization and the length of hospital stay were reduced compared with control groups (Hammarqvist et al. 1989 , Schloerb and Amare 1993 ). A recent clinical study demonstrated reduced 6-mo mortality in critically ill patients with a decrease in treatment costs, comparing glutamine-enriched parenteral nutrition with isonitrogenous isocaloric controls (Griffiths et al. 1997 ).


    Dipeptide concept
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    INTRODUCTION
    Dipeptide concept
    Glutamine dipeptides: a new...
    Implications for glutamine...
    Alternative nitrogen-containing...
    LITERATURE CITED


    The obvious limitations of using glutamine in its native form have initiated an intensive search for amino acid sources and precursors. Indeed, dipeptides are perfect candidates. Their use shows great promise as a method for provision of glutamine, which is otherwise difficult to deliver.

    The dipeptides with glutamine at the C-terminal position, fulfill all chemical and physical criteria needed for approval by the authorities for composition of parenteral solutions.

    Synthesis and characterization of dipeptides with special reference to glutamine containing dipeptides.
    In the early 1980s, dipeptides were not commercially available. Thus, the first task was to synthesize suitable dipeptides on a laboratory scale and attempt a purity of >99%, high water solubility, stability during heat sterilization and storage. In early trials, we used a modified N-carboxy anhydride method for the synthesis of a great variety of peptides in acceptable yields (Stehle et al. 1982 ). Confirmation of the structure of the purified peptides was achieved via mass spectroscopy and nuclear magnetic resonance spectroscopy. Great efforts were made to obtain reliable data concerning peptide purity. We established a novel free-flow electrophoretic technology (analytical isotachophoresis) enabling simultaneous determination of organic and inorganic impurities in the purified peptide material (Stehle et al. 1986 ). The combined use of this highly specific method with reverse-phase HPLC techniques showed purity degrees > 99% for the synthetic peptides. Interestingly, the peptides synthesized revealed solubilities in aqueous solutions 20- to 2000-fold higher than the corresponding free amino acids (Table 1). Heat stability under strictly controlled conditions at 121°C over 30 min was confirmed by heat stability of glutamine and tyrosine peptides (Stehle et al.1982 ). Under these conditions, the cystine-containing peptides showed less stability, yet still retained sufficient stability during sterile filtration to be considered parenteral substrates.




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    Table 1. Chemical/physical characteristics of selected free amino acids and synthetic short chain peptides




    Indeed, using the N-carboxy anhydride method, glutamine-, tyrosine- and cystine-containing dipeptides could be synthesized, yet formation of side products and polymerization reactions diminished product yields and made subsequent purification difficult. Consequently, there was an obvious need for better techniques. As a potential alternative to traditional peptide synthesis procedures, biotechnological approaches using native or immobilized enzymes as biocatalysts have been advocated by peptide chemists. It has been known since the beginning of the 20th century that the protease-catalyzed hydrolysis of peptide bonds is generally reversible. However, it took >50 y until the potentials of this method were recognized and further developed (Konopinska and Muzalewski 1983 , Jakubke et al. 1985 ). The obvious advantages of an enzyme-catalyzed peptide synthesis are the (stereo)-specificity of the reaction, the possibility to minimize protection of functional groups and the feasibility to use free amino acids as nucleophiles. The principle of the kinetic approach using serine or sulfhydryl proteases in aqueous medium is schematically shown in Figure 1 . These enzymes exhibit both hydrolase and esterase activities. In alkaline aqueous solutions, the N-protected amino acid esters (electrophiles) rapidly form the intermediate acyl-enzyme complex. This complex is attacked by nucleophiles, either by water (hydrolysis) or by an amine (aminolysis, e.g., a free amino acid). If k4 (H2N-R) is higher than k3 (H2O), the corresponding N-protected dipeptide is accumulated in the reaction medium. Besides the nucleophile concentration, the ratio aminolysis/hydrolysis additionally can be influenced by pH in the medium reaction temperature and the ratio of nucleophile to electrophile.




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    Figure 1. Schematic illustration of enzyme-catalyzed peptide synthesis (kinetic approach). R-COOX = N-acyl amino acid ester (electrophile); H-E = serine or sulfhydryl protease; H2-N-R = amino acid or derivative thereof; R-CO-E = acyl-enzyme complex. From Fürst et al. 1997a with permission from S. Karger AG, Basel, Switzerland.




    By using commercially available plant (ficin and papain) and animal (chymotrypsin) proteases, we synthesized a great variety of peptide precursors in high yields (Table 2; Stehle et al. 1990 , Monter et al. 1991 ). The use of selectively cleavable N-protecting group (e.g., carbobenzoxy-, formyl-, maleyl-) facilitates an easy and effective liberation of the desired unprotected dipeptide, e.g., simply by acidification of the reaction mixture. After deprotection, the desired dipeptide could be almost quantitatively isolated in high purity (Monter et al. 1991 ).



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    Table 2. Enzyme-catalyzed synthesis of dipeptide precursors




    The prerequisite for a commercial realization of this biotechnological approach is the development of a continuous process. In current studies, we attempted ficin-catalyzed synthesis of the N-protected dipeptide N-carbobenzoxy-L-alanyl-L-glutamine (Cbz-Ala-Gln) using enzyme membrane reactors (reactor volume 10 and 130 mL, respectively; Bahsitta 1993 ). The flow diagram of the experimental system is shown in Figure 2 . The native enzyme is retained in the reactor using an ultrafiltration membrane. Substrate solution 1 (0.2 mol/L Gln, 8 mmol/L EDTA, pH 9.2) was continuously pumped (5–10 mL, residence time: 90 min) through a sterile filter into the thermostatic (30°C) reactor. Before entering the reactor, the glutamine solution was adjusted to pH 9.3–9.5 to maintain an effluent pH of 9.2. Substrate solution 2 (1 mmol/L of the electrophile Cbz-Ala-Ome in EtOH) was periodically added to the reaction mixture every 3 h for 60 min (flow rate: 0.5 mL/h). The reaction was started by adding 100 mg ficin dissolved in water; loss of enzyme activity over time was compensated by periodic addition of 100-mg portions of the enzyme. The mean process time was 60 ± 25 h. At this time, the product yields an average of 45% of theory, which is not yet sufficient to compete with traditional industrial procedures. The results are sufficiently encouraging to justify additional biotechnological approaches for chemical dipeptide synthesis.




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    Figure 2. Flow diagram of the enzyme membrane reactor system. SS1, substrate storage 1; SS2, substrate storage 2 (electrophile); PP, peristaltic pump; TC, titration cell; SF, sterile filter; P, pressure gauge; BT, bubble trap; CSTR, continuously stirred tank reactor (volume 10 mL or 130 mL); PS, product storage. From Fürst et al. 1997a , with permission from S. Karger AG, Basel, Switzerland.





    Glutamine dipeptides: a new dimension in clinical nutrition
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    Glutamine dipeptides: a new...
    Implications for glutamine...
    Alternative nitrogen-containing...
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    Preparations.
    The glutamine containing dipeptides L-alanyl-L-glutamine (Ala-Gln) and glycyl-L-glutamine are available products and today are an integral part of routine clinical practice. These preparations, Dipeptiven and Glamin (Fresenius Kabi, Uppsala, Sweden), are ********** products; the result of many years of intensive research in the field of clinical nutrition. Dipeptiven is a 20% solution of the glutamine-containing dipeptide N(2)-L-alanyl-L-glutamine (Ala-Gln). It is stable during heat sterilization and storage, and it is highly soluble (568 g/L; Table 1 ). Glamin is a complete, well-balanced amino acid solution containing 30.27 g/L stable glycyl-L-glutamine (Gly-Gln). Basic studies in humans and animals provide firm evidence that both glutamine dipeptides are readily used. Importantly, infusion of Dipeptiven or Glamin is well tolerated and not accompanied by any side effects or complaints. The dipeptide concept is based upon the premise that improvement in the quality of available amino acid solutions, currently lacking glutamine, is a major step in resolving the problem of how to formulate and prepare a complete, well-balanced amino acid solution.

    Implications for glutamine dipeptide therapy
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    INTRODUCTION
    Dipeptide concept
    Glutamine dipeptides: a new...
    Implications for glutamine...
    Alternative nitrogen-containing...
    LITERATURE CITED


    Glutamine can be considered a conditionally indispensable amino acid during stress. It is of great importance to formulate guidelines for routine clinical dipeptide nutrition, identifying areas such as:

    which biochemical indications

    which patients

    how much

    when to start administration

    which route of administration

    Biochemical indications.
    Generally, poor nutritional status as assessed by body weight, body mass index, anthropometric measures and low plasma albumin, and severe loss of nitrogen and functional tissue, is a useful indication for glutamine dipeptide therapy. Poor immune status is always a strong signal of glutamine deprivation. Decreased body cell mass, in combination with decreased intracellular and increased extracellular water (easily measured via bioimpedance spectroscopy), favor glutamine dipeptide administration. Please note that plasma-free glutamine concentrations do not always reflect body glutamine status. A normal plasma glutamine level might be associated with severe intracellular glutamine depletion.

    Patients.
    Glutamine (dipeptide) nutrition is an important therapeutic measure in a number of clinical situations. Table 3 suggests patient categories that may benefit from glutamine dipeptide therapy.




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    Table 3. Patient groups that may benefit from glutamine dipeptide therapy




    Timing and route of administration.
    Administration of glutamine by the intravenous route is the most reliable method of achieving a prolonged constant elevation of the free glutamine pool of the body. Supplemental intravenous glutamine dipeptides exert numerous beneficial effects as summarized in Table 4 . Glutamine dipeptides should be provided immediately after the catabolic insult to initially support the attenuated tissues with glutamine.



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    Table 4. Effects of glutamine dipeptide supplemented parenteral nutrition: clinical trials




    At present, there is much controversy concerning the benefit of enteral glutamine nutrition (Fürst 2000b ). In many available studies no convincing biologic or clinical results were obtained from traumatized or intensive care unit (ICU)3 patients despite considerable supply of glutamine (15–35 g/d; Table 5 ).



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    Table 5. Enteral glutamine: clinical studies




    To date, tube-feeding trials show that hypocaloric glutamine-supplemented enteral diets will not provide the requisite amounts of glutamine that can escape the splanchnic bed to elevate blood and muscle concentrations. The reasons for the unfavorable results with enteral glutamine supplementation are multifactorial. Theoretically, the presence of bacterial overgrowth in stressed patients might in part explain the observed low circulating glutamine concentrations, because it is well known that bacteria readily consume glutamine as a preferred substrate. It is also possible that splanchnic glutamine use may contribute to the inability of glutamine-enriched enteral feeds to increase the plasma glutamine levels. Glutamine is absorbed in the upper part of the small intestine and subsequently metabolized in the liver, and, thus, it may not be available in sufficient quantity for the target mucosal tissue at the lower sites of the intestine (Fürst 2000b ) .
    It is notable that enteral glutamine nutrition, which initially did not raise the blood glutamine concentration, has been shown to improve the outcome in premature infants; for example, the frequency of sepsis decreased and immunity increased after 0.3 g/kg body enteral supplementation of glutamine (Neu et al. 1997 ). These beneficial effects presumably reflect increased bowel maturation, indicating that enteral glutamine can act on the gastrointestinal tract without exerting direct systemic effects (Wilmore and Shabert 1998 ). In adult patients, glutamine has been shown to have a beneficial effect on intestinal barrier function when given orally (30 g/d) for several weeks after high dose chemotherapy or radiotherapy for esophageal cancer (Yoshida et al. 1998 ).

    Another confirmation that enteral glutamine is effective in preventing infective complications has been recently reported in 60 patients with severe multiple trauma (Houdijk et al. 1998 ). There was a significant reduction (50%) in the 15-d incidence of pneumonia, bacteremia and severe sepsis. The strengths of this study are in the relatively homogeneous population of patients studied and the fact that the study did not suffer from the confounding factors present in multicenter studies. The results of this fascinating study require confirmation.

    There is some evidence that the body glutamine pool is slower to recover when the same dose of glutamine is given enterally (orally) as opposed to parenterally (Fish et al. 1997 ). The enteral route may be ideal when given early to the noninfected patient to improve gut-associated lymphoid tissue function and immune defense against infection, but for already severely stressed or infected ICU patients, enteral supplements alone may be inadequate, and parallel parenteral support is likely to be required. It has been clearly shown that during intensive care parenteral supplementation of enteral nutrition with glutamine does not increase the risk to the patients and may ensure a better overall outcome (Bauer et al. 1998 ). It should, however, be borne in mind that enteral supplementation with glutamine is a potential hazard because such formulations may form a vigorous cultural medium for microorganisms if strict care is not taken (Griffiths 1999 ).

    Dosing of glutamine dipeptides.
    It is generally accepted that a 60- to 70-kg patient after major injury, uncomplicated elective surgery, with gastrointestinal malfunctions or cachexia, should be given 18–30 g glutamine dipeptides (13–20 g glutamine/d). A severely injured patient with multiple injury, burns, sepsis, systemic inflammatory response syndrome, serious immune deficiency, as well as after bone marrow transplant, may require higher doses of glutamine dipeptide (Wilmore and Shabert 1998 , Griffiths 1999 , Wilmore 1997 , Wilmore et al. 1999 , Fürst et al. 2000b ).

    Indeed, lack of glutamine from conventional TPN and its subsequent supplementation should be considered as a correction of a deficiency rather than as supplementation (Griffiths 1999 , Fürst et al. 1997b ) and as a novel therapeutical measure using glutamine as a pharmacon (pharmacological nutrition). Thus, it is conceivable that the beneficial effects observed with glutamine dipeptide nutrition are simply a correction of disadvantages produced by inadequacies of conventional amino acid solutions. The availability of stable glutamine-dipeptide-containing preparations (Dipeptiven and Glamin) now facilitates glutamine nutrition in routine clinical settings.


    Alternative nitrogen-containing substrates
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    N-acetylated amino acids.
    The implication of N-acetylated amino acids was an early suggestion to facilitate parenteral provision of cysteine, tyrosine and glutamine. Early studies in experimental rats undergoing long-term TPN clearly have shown that highly soluble and stable N-acetylated amino acids, acetylcysteine, acetyltyrosine and acetylglutamine, are rapidly taken up and are subsequently hydrolyzed by acylases after their parenteral administration (Neuhäuser et al. 1985 , 1986 , 1988 ). In a subsequent study in dogs, Abumrad et al. (1989 ) observed only poor use of parenterally supplied acetylglutamine associated with a large urinary excretion (38% of the amount infused). Among the organs studied, only the kidney cleared acetylglutamine to a measurable extent. This was confirmed in healthy humans because continuous infusion of acetylglutamine (Magnusson et al. 1989a ), acetyltyrosine or acetylcysteine (Magnusson et al. 1989b ) resulted in an accumulation of the respective compound in plasma in which levels of the corresponding free amino acids were not, or only slightly, increased (Fig. 3 ). The urinary excretion rate of the acetylated amino acids approached 40–50% of the amount given. After bolus injection of acetyltyrosine, Druml et al. (1991 ) observed little if any hydrolysis of the acetylated amino acid. Pharmacokinetic evaluation after intravenous supply of acetyl-cysteine in humans exhibited an elimination half-life of 2.3 h, a value which is indeed 40-fold higher than values observed for cystine-containing peptides (Stehle et al. 1988 ).





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    Figure 3. Human plasma concentration of acetylglutamine (AcGln), acetyltyrosine (AcTyr) and acetylcysteine (AcCys) before and during intravenous infusion of AcGln, AcTyr and AcCys, respectively. (Modified from Magnusson et al. 1989a and 1989b ).




    It can be concluded that N-acetylated amino acids are poorly used in humans due to restricted acylase capacities except for in the kidneys.
    Short-chain protein hydrolysates.
    Purified short-chain protein hydrolysates (>67% di- and tripeptides, >10% free amino acids) have been discussed as a low osmolality alternative to free amino acid solutions and synthetic dipeptides for peripheral parenteral nutrition (Grimble and Silk 1989 , Grimble et al. 1992 ). In an enzymatically prepared short-chain casein hydrolysate, < 10% of those amino acids that are themselves relatively insoluble or unstable (tyrosine, cysteine, glutamine, tryptophan) were found to exist in free form (Grimble et al. 1987 ).

    During intravenous infusion of a short-chain ovalbumin hydrolysate in healthy human subjects, excess peptide excretion suggested that a large proportion of the hydrolysate was metabolized (Grimble et al. 1988 ). Marked differences between infused and excreted peptide profiles indicated that use of peptides from the hydrolysate was sequence-specific.

    Ornithine -ketoglutarate (OKG).
    The salt OKG might exert a synergistic effect on both its constituents. Recent investigations suggest that after enteral OKG administration gut morphology and function improve, trauma-induced immune dysfunction is alleviated and there are anabolic /anticatabolic actions on protein metabolism (Cynober 1995 , 1999 ). Because the majority of these studies were performed in various experimental models, it is necessary to confirm the postulated benefits in controlled clinical trials. Theoretically, the properties of OKG should counteract the catabolic response that occurs during episodes of infection and after trauma and injury. Enteral administration has been proposed in various catabolic situations (Cynober 1999 ). Favorable effects on muscle protein synthesis have been observed in trauma and burned patients after enteral administration (Cynober 1999 , Le Bricon et al. 1997 ), and improved N-balance and protein synthesis have been found after intravenous administration (Hammarqvist et al. 1991 ). However, direct beneficial effects of ornithine or OKG on gut structure, function or outcome have not been demonstrated (Gardiner et al. 1995 ). Therefore, any clinical impact of the findings outlined above requires confirmation by additional controlled studies (Jolliet et al. 1999 ).

    There are numerous underlying mechanisms proposed that might account for the observed beneficial effects of OKG, including glutamine formation, arginine, proline, polyamine generation, increase in growth hormone and insulin secretion, etc. A principal question is whether OKG is a true precursor for glutamine. According to textbooks, KG is the precursor of glutamic acid, although its precursor function for glutamine is limited. Accordingly, several reports demonstrate that the in vivo transformation from external glutamic acid to glutamine is restricted, corresponding to not > 5–6% of the given dose (Darmaun et al. 1986 ). Certainly labeled KG might be recovered in tissue glutamine (Vaubourdolle et al. 1988 ), yet this finding does not reflect the extent of transformation in a quantitative manner. Human stable-isotope studies confirm that continuous enteral delivery of labeled KG or OKG cannot alter glutamine kinetics in burned patients (Mittendorfer et al. 1999 ). Because glutamic acid is known to be poorly transported across the cell membrane, it can be concluded that KG or related compounds cannot replace glutamine in clinical nutrition unless KG is directly taken up by cells and converted first to glutamic acid and subsequently to glutamine. This theoretical pathway, however, has not yet been established (Fürst et al. 1999 ).

    Adequate delivery of glutamine in the frame of artificial nutrition is an important measure to support healing and reduce morbidity and mortality of stressed patients. Certain clinical conditions are accompanied with characteristic alterations in organ-specific glutamine metabolism. Because the requirement exceeds the availability of glutamine, it should be ranked as conditionally indispensable and, thus, should be a mandatory part of nutritional measures. Apart from its nutritive role, glutamine possesses certain pharmacologic and/or immunologic effects. Clinical studies reveal evidence that the currently applied concept of glutamine nutrition is beneficial in providing patients with a conditionally indispensable amino acid that is otherwise difficult to deliver.

    Among novel ways to deliver glutamine (glutamine dipeptides, acetylglutamine, short-chain protein hydrolysates and OKG), the glutamine dipeptide approach is the most promising. This compilation may well illustrate how far we have advanced our knowledge of the importance of a new substrate in modern artificial nutrition. There is little question that efforts made to modify the response to disease by glutamine nutrition will be rewarded with improved patient outcome.



    FOOTNOTES

    1 Presented at the International Symposium on Glutamine, October 2–3, 2000, Sonesta Beach, Bermuda. The symposium was sponsored by Ajinomoto USA, Inc. The proceedings are published as a supplement to The Journal of Nutrition. Editors for the symposium publication were Douglas W. Wilmore, the Department of Surgery, Brigham and Women’s Hospital, Harvard Medical School and John L. Rombeau, the Department of Surgery, the University of Pennsylvania School of Medicine.

    3 Abbreviations used: ICU, intensive care unit; OKG, ornithine -ketoglutarate.
    Last edited by baller45; 03-03-2004 at 08:19 PM.

  14. #14
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    LITERATURE CITED
    TOP
    ABSTRACT
    INTRODUCTION
    Dipeptide concept
    Glutamine dipeptides: a new...
    Implications for glutamine...
    Alternative nitrogen-containing...
    LITERATURE CITED




    Abumrad N. N., Morse E. L., Lochs H., Williams P. E. & Adibi S. A. (1989) Possible sources of glutamine for parenteral nutrition: impact on glutamine metabolism. Am. J. Physiol. 257:E228-E234.[Medline]
    Anderson P. M., Schroeder G. & Skubitz K. M. (1998) Oral glutamine reduces the duration and severity of stomatitis after cytotoxic cancer chemotherapy. Cancer 83:1433-1439.[Medline]
    Bahsitta H.-P. (1993) Enzym-katalysierte synthese von glutaminhaltigen dipeptiden unter verwendung von immobilisiertem ficin als biokatalysator. Doctoral thesis 1993 Universität Hohenheim Stuttgart, Germany. .
    Barua J. M., Wilson E., Downie S., Weryk B., Cuschieri A. & Rennie M. J. (1992) The effect of alanyl-glutamine peptide supplementation on muscle protein synthesis in post-surgical patients receiving glutamine-free amino acids intravenously. Proc. Nutr. Soc. 51:104A.
    Bauer P., Charpentier C., Bouchet C., Raffy F., Caconnet N. & Larcan A. (1998) Short parenteral nutrition coupled with early enteral nutrition in the critically ill. Intensive Care Med 24(suppl.):123.
    Bozzetti F., Biganzoli L., Gavazzi C., Cappuzzo F., Carnaghi C., Buzzoni , Dibartolomeo M. & Baietta E. (1997) Glutamine supplementation in cancer patients receiving chemotherapy—a double-blind randomized study. Nutrition 13:748-751.[Medline]
    Conversano L., Muscaritoli M., Petti M. C, Cangiano C., Cascino A., Laviano A., Micozzi A., Preziosa I., Torelli G. F. & Falcone C. (1995) Effects of oral glutamine on high-dose chemotherapy (HDCT)-induced gastrointestinal toxicity in acute leukemia patients: a pilot study. Clin. Nutr. 14(suppl. 2):6.
    Cynober L. A. (1995) Understanding the pathological mechanisms underlying protein breakdown for new therapeutic strategies (editorial). Nutrition 11:398.[Medline]
    Cynober L. A. (1999) The use of -ketoglutarate salts in clinical nutrition and metabolic care. Curr. Opin. Clin. Nutr. Metab. Care 2:33-38.[Medline]
    de Beaux A. C., O’Riordain M. G., Ross J. A., Jodozi L., Carter D. C. & Fearon K. C. (1998) Glutamine supplemented total parenteral nutrition reduces blood mononuclear cell interleukin-8 release in severe acute pancreatitis. Nutrition 14:261-265.[Medline]
    Darmaun D., Matthews D. E. & Bier D. M. (1986) Glutamine and glutamine kinetics in humans. Am. J. Physiol. 251:E117-E126.[Medline]
    Druml W., Lochs H., Roth E., Hübl W., Balcke P. & Lenz K. (1991) Utilization of tyrosine dipeptides and acetyltyrosine in normal and uremic humans. Am. J. Physiol. 260:E280-E285.[Medline]
    Earl S., Wood D. & Gardner M.L.G. (1995) The effects of elemental diets and glutamine supplementation on intestinal absorptive function. Clin. Nutr. 14:134-140.
    Fish J., Sporay G. & Beyer K. (1997) A prospective randomized study of glutamine-enriched parenteral nutrition compared with enteral feeding in postoperative patients. Am. J. Clin. Nutr. 65:977-983.[Abstract]
    Fürst P. (2000a) Jonathan E. Rhoads lecture: a thirty year odyssey in nitrogen metabolism from ammonium to dipeptides. J. Parenter. Enteral Nutr 24:197-209.[Medline]
    Fürst P. (2000b) Conditionally indispensable amino acids (glutamine, cyst(e)ine, tyrosine, arginine, ornithine, taurine) in enteral feeding and the dipeptide concept. Proteins, Peptides and Amino Acids in Enteral Nutrition. Nestlé Nutrition Workshop Series Clinical & Performance Programme 2000b:199-219 Nestec Ltd. Vevey/S. Karger Basel, Switzerland. .
    Fürst P., Pogan K., Hummel M., Herzog B. & Stehle P. (1997a) Reappraisal of indispensable amino acid: design of parenteral synthetic dipeptides for clinical nutrition: Synthesis and characterization. Ann. Nutr. Metab. 41:1-9.[Medline]
    Fürst P., Albers S. & Stehle P. (1990) Glutamine-containing dipeptides in parenteral nutrition. J. Parenter. Enteral Nutr. 14:118S-124S.[Medline]
    Fürst P., Pogan K. & Stehle P. (1997b) Glutamine dipeptides in clinical nutrition. Nutrition 13:731-737.[Medline]
    Fürst P., Kuhn K. S. & Ziegler T. R. (1999) Amino acids and proteins–new definitions and requirements, hormonal interactions, methodological advances and pitfalls: editorial comment. Curr. Opin. Clin. Nutr. Metab. Care 2:5-8.[Medline]
    Fürst P., Kuhn K. S. & Stehle P. (2000a) New nitrogen-containing substrates in artificial nutrition. Pichard C. Kudsk K. A. eds. From Nutrition Support to Pharmacologic Nutrition in the ICU: Update in Intensive Care and Emergency Medicine 2000a:441-460 Vevey/S. Karger Basel, Switzerland. .
    Fürst P., Kuhn K. S. & Stehle P. (2000b) New nitrogen-containing substrates in artificial nutrition. Pichard C. Kudsk K. A. eds. From Nutrition Support to Pharmacologic Nutrition in the ICU: Update in Intensive Care and Emergency Medicine 2000b:441-460 S. Karger Basel, Switzerland. .
    Gardiner K. R., Kirk S. J. & Rowlands B. J. (1995) Novel substrates to maintain gut integrity. Nutr. Res. Rev. 8:43-66.
    Griffiths R. D., Jones C. & Palmer T.E.A. (1997) Six-month outcome of critically ill patients given glutamine-supplemented parenteral nutrition. Nutrition 13:295-302.[Medline]
    Griffiths R. D. (1999) Glutamine: establishing clinical indications. Curr. Opin. Clin. Nutr. Metab. Care 2:177-182.[Medline]
    Grimble G. K., Rees R. G., Keohane P. P., Cartwright T., Desreumaux M. & Silk D. A. (1987) Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum. Gastroenterology 92:135-142.
    Grimble G. K., Raimundo A., Rees R. G., Hunjan M. K. & Silk D. A. (1988) Parenteral utilization of a purified short-chain enzymic hydrolysate of ovalbumin in man. J. Parenter. Enteral Nutr. 12(suppl.):15S.
    Grimble G. K. & Silk D. A. (1989) Peptides in human nutrition. Nutr. Res. Rev. 2:87-108.
    Grimble G. K., Aimer P. C., Morris P., Raimundo A., Weryk B. & Silk D. A. (1992) Plasma amino acids and peptiduria during intravenous infusion of a short-chain ovalbumin hydrolysate, or its equivalent amino acid (AA) mixture, in man. Proc. Nutr. Soc. 51:103A.
    Hammarqvist F., Wernerman J., Ali R., Von der Decken A. & Vinnars E. (1989) Addition of glutamine to total parenteral nutrition after elective abdominal surgery spaces free glutamine in muscle, counteracts the fall in muscle protein synthesis, and improves nitrogen balance. Ann. Surg. 209:455-461.[Medline]
    Hammarqvist F., Wernerman J., Von der Decken A. & Vinnars E. (1990) Alanyl-glutamine counteracts the depletion of free glutamine and the postoperative decline in protein synthesis in skeletal muscle. Ann. Surg. 212:637-644.[Medline]
    Hammarqvist F., Wernerman J., Von der Decken A. & Vinnars E. (1991) -ketoglutarate preserves protein synthesis and free glutamine in skeletal muscle after surgery. Surgery 109:28-36.[Medline]
    Hankard R. G., Hammond D., Haymond M. W. & Darmaun D. (1998) Oral glutamine slows down whole body protein breakdown in Duchenne muscular dystrophy. Pediatr. Res. 43:222-226.[Abstract]
    Houdijk A.P.J. (1998) Glutamine-enriched enteral nutrition in patients with multiple trauma. Lancet 352:1553.[Medline]
    Houdijk A. P., Rijnsburger E. R., Jansen J., Wesdorp R. I., Weiss J. K., McCamish M. A., Teerlink T., Meuwissen S. G., Haarman H. J. & Thijs L. G. (1998) Randomised trial of glutamine-enriched enteral nutrition on infectious morbidity in patients with multiple trauma. Lancet 352:772-776.[Medline]
    Jakubke H.-D., Kuhl P. & Könnecke A. (1985) Basic principles of protease-catalyzed peptide bond formation. Angew Chem. Int. Ed. 24:85-93.
    Jolliet P., Biolo G. & Chiolero R. (1999) Enteral nutrition in intensive care patients: a practical approach. Clin. Nutr. 18:47-56.[Medline]
    Jones C., Palmer T. E. & Griffiths R. D. (1999) Randomized clinical outcome study of critically ill patients given glutamine-supplemented enteral nutrition. Nutrition 15:108-115.[Medline]
    Karner J., Roth E., Stehle P., Albers S. & Fürst P. (1989) Influence of glutamine-containing dipeptides on muscle amino acid metabolism. Hartig W. Dietze G. Weiner R. Fürst P. eds. Nutrition in Clinical Practice 1989:56-70 Karger Basel, Switzerland. .
    Khan K., Hardy G., McElroy B. & Elia M. (1991) The stability of L-glutamine in total parenteral nutrition solutions. Clin. Nutr. 10:193-198.
    Konopinska D. & Muzalewski F. (1983) Proteolytic enzymes in peptide synthesis. Mol. Cell. Biochem. 51:165-175.[Medline]
    Le Bricon T., Coudray-Lucas C., Lioret N., Lim S. K., Plassart F., Schlegel L., De Bandt J. P., Saizy R., Giboudeau J. & Cynober L. (1997) Ornithine -ketoglutarate metabolism after enteral administration in burn patients: bolus compared with continuous infusion. Am. J. Clin. Nutr. 65:512-518.[Abstract]
    Li J., Kudsk K. A., Janu P. & Renegar K. B. (1997) Effect of glutamine-enriched total parenteral nutrition on small intestinal gut-associated lymphoid tissue and upper respiratory tract immunity. Surgery 121:542-549.[Medline]
    Magnusson I., Kihlberg R., Alvestrand A., Wernerman J., Ekman L. & Wahren J. (1989a) Utilization of intravenously administered N-acetyl-L-glutamine in humans. Metabolism 38(suppl. 1):82-88.[Medline]
    Magnusson I., Ekman L., Wangdahl M. & Wahren J. (1989b) N-acetyl-L-tyrosine and N-acetyl-L-cysteine as tyrosine and cysteine precursors during intravenous infusion in humans. Metabolism 38:957-961.[Medline]
    Mittendorfer B., Gore D. C., Herndon D. N. & Wolfe R. R. (1999) Accelerated glutamine synthesis in critically ill patients cannot maintain normal intramuscular free glutamine concentration. J. Parenter. Enteral Nutr. 23:243-250.[Medline]
    Monter B., Herzog B., Stehle P. & Fürst P. (1991) Kinetically controlled synthesis of dipeptides using ficin as biocatalyst. Biotechnol. Appl. Biochem. 14:183-191.[Medline]
    Morlion B. J., Köller M., Wachtler P., Wrenger K., Fürst P., Puchstein C. & König W. (1997) Influence of L-alanyl-L-glutamine (ala-gln) dipeptide on the synthesis of leukotrienes and cytokines in vitro. Proceedings of the 4th International Congress on the Immune Consequences of Trauma, Shock and Sepsis 1997:269-272 Monduzzi Editore S.p.A Bologna, Italy .
    Morlion B. J., Stehle P., Wachtler P., Siedhoff H. P., Köller M., König W., Fürst P. & Puchstein C. (1998) Total parenteral nutrition with glutamine dipeptide after major abdominal surgery: a randomized, double-blind, controlled study. Ann. Surg. 220:212-221.
    Nattakom T. V., Charlton A. & Wilmore D. W. (1995) Use of vitamin E and glutamine in the successful treatment of severe veno-occlusive disease following bone marrow transplantation. Nutr. Clin. Prac. 10:16-18.
    Neu J., Roig J. C., Meetze W. H., Veerman M., Carter C., Millsaps M., Bowling D., Dallas M. J., Sleasman J. & Knight T. (1997) Enteral glutamine supplementation for very low birth weight infants decreases morbidity. J. Pediatr. 131:691-699.[Medline]
    Neuhäuser M., Wandira J. A., Göttmann U., Bässler K. H. & Langer K. (1985) Utilization of N-acetyl-L-tyrosine and glycyl-L-tyrosine during long-term parenteral nutrition in the growing rat. Am. J. Clin. Nutr. 42:585-596.[Abstract]
    Neuhäuser M., Grötz K. A., Wandira J. A., Bässler K. H. & Langer K. (1986) Utilization of methionine and N-acetyl-L-cysteine during long-term parenteral nutrition in the growing rat. Metabolism 35:869-873.[Medline]
    Neuhäuser M., Wirth S., Hellmann U. & Bässler K. H. (1988) Utilization of N-acetyl-L-glutamine during long-term parenteral nutrition in growing rats: significance of glutamine for weight and nitrogen balance. Clin. Nutr. 7:145-150.
    O’Riordain M., Fearon K. C., Ross J. A., Rogers P., Falconer J. S., Bartolo D. C., Garden O. J. & Carter D. C. (1994) Glutamine supplemented total parenteral nutrition enhances T-lymphocyte response in surgical patients undergoing colorectal resection. Ann. Surg. 220:212-221.[Medline]
    Petersson B., Walle R.S.O., Von der Decken A., Vinnars E. & Wernerman J. (1991) The long-term effect of postoperative TPN supplemented with glycyl-glutamine on protein synthesis in skeletal muscle. Clin. Nutr. 10(suppl. 2):10(abs.).
    Roig J. C., Bowling D. & Dallas M. (1995) Enteral Glutamine Supplementation Decreases Nosocomial Infection and Alters T-cell Subset in the Very Low Birth Weight (VLBW) (< 1250 Gram) Neonate 1995 Congress of the American Pediatric Society .
    Roig J. C., Meetze W. H., Auestad N., Jasionowski T., Veerman M., McMurray C. A. & Neu J. (1996) Enteral glutamine supplementation for the very low birth weight infant: plasma amino acid concentrations. J. Nutr. 126(suppl. 11):15S-20S.
    Rubio I. T., Cao Y., Hutchins L. F., Westbrook K. C. & Klimberg V. S. (1998) Effect of glutamine on methotrexate efficacy and toxicity. Ann. Surg. 227:772-778.[Medline]
    Schloerb P. R. & Amare M. (1993) Total parenteral nutrition with glutamine in bone marrow transplantation and other clinical applications (a randomized, double-blind study). J. Parenter. Enteral Nutr. 17:407-413.[Medline]
    Schloerb P. R. & Skikne B. S. (1999) Oral and parenteral glutamine in bone marrow transplantation: a randomized, double-blind study. J. Parenter. Enteral Nutr. 23:117-122.[Medline]
    Shive W., Snider R. N., DuBilier B., Rude J. C., Clarke G. E. & Ravel J. O. (1957) Glutamine treatment of peptic ulcer. Tex. State J. Med. 11:840.
    Skubitz K. M. & Andersen P. M. (1996) Oral glutamine to prevent chemotherapy induced stomatitits: a pilot study. J. Lab. Clin. Med. 127:223-228.[Medline]
    Stehle P., Kühne B., Kubin W., Fürst P. & Pfaender P. (1982) Synthesis and characterisation of tyrosine- and glutamine-containing peptides. J. Appl. Biochem. 4:280-286.
    Stehle P., Bahsitta H.-P. & Fürst P. (1986) Analytical control of enzyme-catalyzed peptide synthesis using capillary isotachophoresis. J. Chromatogr. 370:131-138.
    Stehle P., Albers S., Pollack L. & Fürst P. (1988) In vivo utilization of cystine-containing synthetic short chain peptides after intravenous bolus injection in the rat. J. Nutr. 118:1470-1474.[Medline]
    Stehle P., Zander J., Mertes N., Albers S., Puchstein C. H., Lawin P. & Fürst P. (1989) Effect of parenteral glutamine peptide supplements on muscle glutamine loss and nitrogen balance after major surgery. Lancet 1:231-233.[Medline]
    Stehle P., Bahsitta H.-P., Monter B. & Fürst P. (1990) Papain-catalyzed synthesis of dipeptides: a novel approach using free amino acids as nucleophiles. Enzyme. Microb. Technol. 12:56-60.[Medline]
    Van der Hulst R.R.W.J., Van Kreel B. K., Von Meyenfeldt M. F., Brummer R. J., Arends J. W., Deutz N. E. & Soeters P. B. (1993) Glutamine and the preservation of gut integrity. Lancet 431:1363-1365.
    Van Zaanen H.C.T., Van der Lilie J., Timmer J. G., Fürst P. & Sauerwein H. P. (1994) Parenteral glutamine supplementation does not ameliorate chemotherapy-induced toxicity. Cancer 74:2879-2884.[Medline]
    Vaubourdolle M., Jardel A., Coudray-Lucas C., Ekindijan O. G., Agneray J. & Cynober L. (1988) Metabolism and kinetics of parenterally administered ornithine and -ketoglutarate in healthy and burned animals. Clin. Nutr. 7:105-111.
    Wilmore D. W. & Shabert J. K. (1998) Role of glutamine in immunologic responses. Nutrition 14:618-626.[Medline]
    Wilmore D. W. (1997) Glutamine saves lives! What does it mean?. Nutrition 13:375-387.[Medline]
    Wilmore D. W., Schloerb P. R. & Ziegler T. R. (1999) Glutamine in the support of patients following bone marrow transplantation. Curr. Opin. Clin. Nutr. Med. Care 2:323-328.
    Wischmeyer P., Pemberton J. H. & Phillips S. F. (1993) Chronic pouchitis after ileal pouch-anal anastomosis: responses to butyrate and glutamine suppositories in a pilot study. Mayo Clin. Proc. 68:978-981.[Medline]
    Yoshida S., Matsui M., Shirouzu Y., Fujita H., Yamana H. & Shirouzu K. (1998) Effects of glutamine supplements and radiochemotherapy on systemic immune and gut barrier function in patients with advanced esophageal cancer. Ann. Surg. 227:485-491.[Medline]
    Ziegler T. R., Benfell K., Smith R. J., Young L. S., Brown E., Ferrari-Balliviera E., Lowe D. K. & Wilmore D. W. (1990) Safety and metabolic effects of L-glutamine administration in humans. J. Parenter. Enteral Nutr. 14:137S-146S.[Medline]
    Ziegler T. R., Young L. S., Benfell K., Scheltinga M., Hortos K., Bye R., Morrow F. D., Jacobs D. O., Smith R. J., Antin J. H. & Wilmore D. W. (1992) Clinical and metabolic efficacy of glutamine-supplemented parenteral nutrition after bone marrow transplantation: a randomized, double-blind controlled study. Ann. Intern. Med. 116:821-828.[Medline]
    Zoli G., Care F. & Falco C. (1995) Effect of oral glutamine on intestinal permeability and nutritional status in Crohn’s disease. Gastroenterology 108:A766.

  15. #15
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    so...

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    Holy ****! You just solved the great glutamine debate. Tell all the mods! We have the answer! We found the study! Glutamine is useless! Burn the church!

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    i hate when ppl paste something thats half a mile long, if you already read it, give us the short of it, or just post the site link..... the more glut u take a day the more you absorb, you also waste more as well, but you still can take as much as you like really.

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    Quote Originally Posted by Elliot
    caps are horrible its a total rip off.. get protein powder that already has it.. www.allthewhey.com for example..
    also agree. but some dont give adequate amounts, and some have none at all.

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    5 gram postw & 5 gram before bed seems to work fine for me..

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    Just keep this in mind. If you are taking in protein drinks each day, then there is most likely no need for glutamine. But if your not, then get some...

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    Quote Originally Posted by daman1
    Just keep this in mind. If you are taking in protein drinks each day, then there is most likely no need for glutamine. But if your not, then get some...
    True. Glutamine is manufactured in your body from amino acids I believe. Or you can be like me and have glutamine mixed in your protein.

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    Quote Originally Posted by decadbal
    i hate when ppl paste something thats half a mile long, if you already read it, give us the short of it, or just post the site link..... the more glut u take a day the more you absorb, you also waste more as well, but you still can take as much as you like really.
    I would have but you don't have access to the site its from.
    I wish someone would have read the study. It says that a peptide like l-alanyl-l-glutamine is something that would give you the benefits your looking for from normal glutamine. The get sucked away by your intestine. Unless you are sick. People who are ill are able to get benifits from free form glutamine.

    Quote Originally Posted by RP7
    Glutamine is manufactured in your body from amino acids I believe.
    Yep it's synthesized from glutamate and glutamic acid by glutamate-ammonia ligase. Thats why a good protein shake is enough.
    Last edited by baller45; 03-08-2004 at 12:36 AM.

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    Quote Originally Posted by baller45
    Unless you are sick. People who are ill are able to get benifits from free form glutamine.
    Now you seem to be somewhat contradicting yourself. Since intense workouts depress the immune system albeit temporarily and also reduce glutamine stores, then how is free form glutamine not beneficial for us all?

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    Quote Originally Posted by RP7
    Now you seem to be somewhat contradicting yourself. Since intense workouts depress the immune system albeit temporarily and also reduce glutamine stores, then how is free form glutamine not beneficial for us all?
    I didn't mean a temp drop in the immune system. I mean so bad that the absorbtion of the free form is due to the body own surival mechanism kicking in. Anyway, a good protein shake will be plenty to top off your stores.
    Those studies that use hospital patients are very commonly used by supplement companies to push the benefits of free form. You just got to check up on their references to see just what group of people got those results.

    The worst is when they will site studies about that methoxy stuff.
    They are almost all completley done on geriatrics.

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