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Mario V. Fringes

Beiträge: 845
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Registriert: 29.05.2001

14.03.2003 15:19     Profil von Mario V. Fringes   Mario V. Fringes eine Nachricht schreiben     Beitrag editieren/löschen
Verkaufe [b:b734e7add8]10 x 1 kg Glutaminpeptid[/b:b734e7add8] von [b:b734e7add8]KiloSports[/b:b734e7add8] für jeweils 50,- Eur plus Versand. Bitte beachten: Das ist [b:b734e7add8]kein billiges L-Glutamin[/b:b734e7add8], sondern [b:b734e7add8]reines Glutaminpeptid[/b:b734e7add8]. Kein Zucker, kein Garnichts! Reines Glutaminpeptid! Bei Interesse könnt ihr mich unter mario@p-p-e.com anmailen! Gruß, [i:b734e7add8]Mario V. Fringes[/i:b734e7add8] PPE CS

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Mario V. Fringes

Beiträge: 845
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Registriert: 29.05.2001

14.03.2003 15:22     Profil von Mario V. Fringes   Mario V. Fringes eine Nachricht schreiben     Beitrag editieren/löschen
Ach so, Verwendungszweck: Vor allem als anti-kataboler Faktor während Diätphasen einsetzbar. Hier sind noch einige Infos: [list:b7a0df736f]Glutamine peptides are a naturally rich, stable source of glutamine. Glutamine is as dietary nonessential amino acid. One of the most abundant and versatile amino acids in the body, glutamine has long enjoyed use by bodybuilders and similarly focused athletes, as well as many nonathletes. Glutamine is frequently used post-exercise to promote recovery of exercised muscle tissue (e.g., replenishment of glycogen stores), enhance muscle growth, and support immune system function (e.g., following prolonged exhaustive distance running). Below are listed some of the many potentially valuable properties of this versatile amino acid: L-Glutamine and Glycogen Glutamine is a key precursor to glucose, more important quantitatively than alanine (Nurjhan et al., 1995; Stumvoll et al., 1999). Glutamine stimulates gluconeogenesis as well as glycogen formation (Bowtell et al., 1999). It is a major source of glucose used for skeletal muscle glycogen and hepatic (liver) glycogen synthesis, such as during recovery from exercise (Bowtell et al., 1999). Glutamine has been found to promote anabolism in skeletal muscle of both animals and healthy humans. These effects include enhancement of the syntheses of both glycogen (Varnier et al., 1995; Low et al., 1996a; 1996b; Bowtell et al., 1999) and protein (MacLennan et al., 1988; Barua et al., 1992). Anabolic effects on muscle glycogen may relate to glutamines observed cell-volumizing properties (Low et al, 1996b). Cell volumization is thought to play an important role in the control of anabolic processes. Post-exercise, glutamine supplementation accelerates the recovery of depleted skelelal muscle and hepatic (liver) glycogen (Varnier et al., 1995; Bowtell et al., 1999) as powerfully as carbohydrate. This may allow glycogen recovery to occur on a carbohydrate-restricted diet. In healthy subjects consuming 5-8 grams of glutamine post-exercise, both liver and muscle glycogen resynthesis may be accelerated (Bowtell et al., 1999), thereby assisting in recovery from training and sparing endogenous (e.g., intramuscular) glutamine. In humans, glutamine plays a major role as a source of glucose for maintaining hepatic glycogen stores (Nurjhan et al., 1995). Carbohydrate-restricted diets are often associated with a depletion of liver glycogen and, consequently, ATP availability. A glycogen-depletion-induced decline in liver ATP supply may contribute to the low T3 (active thyroid hormone) levels, and associated suppression of metabolic rate and fat loss, seen on low-calorie and/or low-carbohydrate diets. Thus, glutamine supplementation may help to preserve metabolic rate under low-calorie and/or low-carbohydrate dietary conditions. General Information on Glutamine Glutamine is the most abundant amino acid in the body, i.e., both intra- and extra-cellularly (de Vasconcelos and Tirapegui, 1998) Excluding taurine, glutamine makes up more than half of the free amino acid pool in muscle (Bergstrom et al., 1974; Hankard et al., 1995). Skeletal muscle contributes 50-80% of the free amino acid pool of the body. The intracellular concentration of glutamine is ~20 mmol/L (Bergstrum et al. 1974), with an intra-/extracellular transmembrane gradient of 30. Glutamine-producing tissues include skeletal muscle, brain, heart, lungs, skin, and adipose tissue (van Acker, 1999). Skeletal muscle contains more glutamine synthetase activity than that of glutaminase, rendering it a net producer of glutamine. Glutamine synthetase catalyzes the ATP-dependent addition of ammonia (e.g., as from the catabolism of BCAA) to glutamine to produce glutamine. Concerning BCAAs, hyperammonemia indirectly lowers the plasma levels of BCAA by stimulating glutamine synthesis, thus reducing the intracellular glutamate pool, which is likely to be restored, at least in part, by an intensified BCAA transamination. Clarification is needed as to whether carbon skeletons derived from valine and isoleucine additionally contribute to replenishing the glutamate pool. Glutamine is a conditionally essential amino acid, meaning that the body's demand for it can exceed the supply under certain stressful conditions. The largest site of glutamine in the body is skeletal muscle (Bergstrom et al., 1974). Under normal conditions, intramuscular synthesis of glutamine (e.g., using ammonia derived from BCAA catabolismin) and protein catabolism maintain intramuscular glutamine levels by balancing the release of glutamine (Mittendorfer et al., 1998). Whole-body glutamine appearance in plasma may amount to up to 60-100 g per day for a 70-kg man (Nurjhan et al., 1995) Tracer studies indicated that skeletal muscle accounts for ~70% of the post-absorptive glutamine turnover rate; the contribution of de novo synthesis being estimated at ~60%. Indirect estimation of the glutamine de novo synthetic rate in muscle tissue requests the knowledge of the rate of glutamine appearance into plasma and the share of glutamine derived from intracellular protein degradation; the latter can only be obtained by considering the content of glutamine in mixed muscle protein. L-Glutamine Transport Glutamine stimulates the activity of its specific transporter, thereby affecting an increase in nitrogen delivery. In animals fed a glutamine-enriched diet, glutamine increased the activity of glutamine transporter System N 75% compared to animals fed the control diet (Salloum et al., 1990). Glutamine transport into muscle occurs largely via an insulin-sensitive transporter; hence, improving insulin sensitivity may act synergistically with glutamine supplementation to achieve muscle anabolism The major transporter for glutamine in sketetal muscle is the Na+-dependent, insulin-sensitive System Nm. When intracellular glutamine concentrations decrease, the activity of this transporter is increased; conversely, System Nm activity is down-regulated as glutamine concentrations are re-established (Tadros et al., 1993). L-Glutamine as a Conditionally Essential Amino Acid Despite glutamine's "non-essential" classification, all cells require this amino acid to function. Within cells, glutamine plays a role in synthesizing the purine building blocks of RNA and DNA; along with glycine and folic acid, glutamine is utilized during de novo purine biosynthesis. Glutamine is a principal metabolic substrate for tissues characterized by rapidly replicating cells, such as enterocytes, immune cells, granulation tissue, and keratinocytes. Under various conditions of stress, glutamine use in these tissues is accelerated to the point that it may become essential; hence the term "conditionally essential". Besides its role in cell division, glutamine functions to transport carbon and nitrogen between tissues; it is an important precursor for urea synthesis in the liver, ammonia production in the kidney, and for both hepatic and renal gluconeogenesis. In addition, a number of cell types utilize large amounts of glutamine as the major respiratory fuel, channeling its carbon skeleton into the citric acid cycle for production of ATP. In fibroblasts, for instance, the transported glutamine is used primarily for energy production via oxidation of glutamine carbons to carbon dioxide. An increase in protein anabolism as a result of GH and IGF-I treatment may result in a decrease in glutamine availability, exacerbating the glutamine depletion seen in the critically ill. L-Glutamine and Protein Synthesis Glutamine potentiates the protein anabolic effects of leucine (Hankard et al., 1996), and is itself an important regulator of muscle protein synthesis A striking correlation has been reported between the size of muscle free glutamine pool and rates of protein synthesis in animal studies (Jepson et al., 1988). This correlation is specific for glutamine and has not been observed with any other amino acid (Jepson et al., 1988) Glutamine, as well as leucine, potently stimulates protein S6 kinase (Iiboshi et al., 1999), a key enzyme involved in the regulation of protein synthesis in skeletal muscle and other tissues. Recall also that glutamine potentiates the protein anabolic effects of leucine. Whole-body glutamine appearance in plasma may amount to up to 60-100 g per day for a 70-kg man (Nurjhan et al., 1995); in order to affect a change in muscle protein anabolism, large (multi-gram) quantities of glutamine may be required. L-Glutamine and Cortisol, Protein Catabolism Glutamine synthetase (GS), a key enzyme for glutamine synthesis in muscle is upregulated by glucocorticoids (Meynial-Denis et al., 1996). Glutamine supplementation inhibits glucocorticoid-inudced GS activity (Hickson eta l., 1996). During fasting, the skeletal muscle responds by exporting increased amounts of glutamine (and alanine), irrespective of the species studied (Cersosimo et al., 1986). This response reflects an increased activity of GS in skeletal muscle in order to maintain muscle glutamine pool. GS regulation in skeletal muscle is adrenal-dependent in both fed and fasted animals. Cersosimo et al. (1986) found that four days of fasting in rats produced ketosis with a compensated metabolic acidosis. The demand for glutamine by the kidneys and gut increased, and the liver switched from net glutamine utilization to that of net production. The liver, by becoming a net producer of glutamine, and the kidney, by increasing its production of alanine, decrease demands for peripheral release of these two amino acids, and thus may have protein-sparing actions during fasting. L-Glutamine and Nitric Oxide (NO) Glutamine is a major precursor to the NO precursor, arginine (Windmueller and Spaeth, 1975; 1978). Glutamine is supplied from the muscle to the small intestine for citrulline synthesis. Citrulline synthesized from glutamate in the small intestine is converted into arginine in the kidney, arginine is supplied to various tissues and then converted into ornithine in the liver. The synthesis of citrulline from glutamate is carried out by the reversal of the ornithine aminotransferase reaction. L-Glutamine and Thermogenesis In healthy humans, glutamine affects a marked increase in energy expenditure when administered enterally (Hankard et al., 1996). Infusion of this amino acid was associated with a ~17% increase in resting energy expenditure (REE), from 1531 kcal/day to 1842 kcal/day. Glycine infusion, by contrast, produced no significant change in REE. Glutamine, but not glycine, was also shown to stimulate protein synthesis in the healthy subjects used for the study. The authors relate: The present study suggests that, in healthy adult subjects, glutamine administration is associated with an increase in protein synthesis. The observed increase in resting energy expenditure with glutamine is consistent with such an increase in protein synthesis, as protein synthesis is an energy costly process. Assuming the cost of protein synthesis as 20% of energy expenditure, the 7% increase in protein synthesis should elicit a 1.4% increase in energy expenditure (0.20 x 7% = 1.4%); the increase in energy expenditure observed upon infusion of glutamine therefore cannot be entirely accounted for by enhanced protein synthesis. The complete oxidation of glutamine: Glutamine + 5O2 5 CO2 + 3H2O + 2 NH3 L-Glutamine and Thyroid Hormones, Metabolic Rate Current evidence indicates that T3 is the key active thyroid hormone; its production has therefore received more attention than other deiodinative iodothyronine degradations. Approximately 80% of the circulating T3 is produced peripherally, i.e., in extra-thyroidal tissues, by the removal of a 5 iodine from T4 by the activity of 5 deiodinase, in rats and humans (Engler and Burger, 1984). The conversion of T4 to T3 appears to require glutathione (GSH) (Sato et al., 1982), and involves (and may indeed be rate-limited by) the active transport of T4 into liver cells by a process dependent on intracellular ATP (De Jong et al., 1994). Healthy humans fed very-low carbohydrate diets for 4 days experience a substantial decrease in T3 levels (Fery et al., 1982). The decreases in circulating T3 concentrations under such dietary conditions, and with fasting, result primarily from alterations in T4 deiodination (Danforth, 1986). T4 deiodination cannot be restored simply by providing additional T4. However, studies of the regulation of hepatic 5 deiodination during nutritional alterations reveal that glucose and insulin (via different mechanisms) are capable of reversing the effects of fasting on T3 production. Provision of a carbohydrate diet stimulates hepatic 5 deiodinase activity by increasing the tissue enzyme content (Gavin et al., 1981). These data are not surprising inasmuch as depletion of ATP may be expected by interference with glycolysis (as with dietary carbohydrate restriction or fasting), resulting in a lack of oxidizable substrates for ATP generation. Thus, a carbohydrate-restricted diet may impair T3 production, and, consequently, reduce metabolic rate. Glutamine, by serving as a key non-carbohydrate source of glucose, and stimulating glycogen synthesis, possibly via liver cell volumization (Lavoinne et al., 1998), supports intracellular ATP levels, and therefore, T4 uptake and conversion to T3. Further, as glutamine levels in liver and muscle (Hammarqvist et al., 1997) are associated with glutathione status (i.e., a fall in muscle glutamine content is associated with a decrease in muscle GSH), supplementation with this amino acid may be important in supporting maximal GSH-dependent activity of the 5 deiodinating enzymatic machinery, alongside its protein anabolic effects (Hammarqvist et al., 1997). L-Glutamine and Skeletal Muscle Skeletal muscle, with the highest level of free glutamine, is perhaps the most important source of this amino acid and releases the compound for removal by other organ tracts, such as the gastrointestinal tract, during the postabsorptive state. Glutamine produced by muscle is an important fuel and regulator of DNA and RNA synthesis in mucosal cells and immune system cells and fulfils several other important functions in human metabolism. Glutamine appears to be involved in the regulation of a number of important metabolic processes in skeletal muscle and heart muscle (e.g., regulation of the reduced/oxidized gluathione ratio; GSH/GSSG) and regulation of protein and glycogen synthesis). Furthermore, glutamine transport appears to interact with systems for regulation of volume control and many of the metabolic features attributable to changes in glutamine concentration appear to be modulated via alteration in cytoskeletal status. Bevan et al. (1991) investigated the effect of changes in cell volume on the rates of release of glutamine and alanine from muscle and on the concentrations of these amino acids in muscle. Their results suggested that cell volume may play a role in the regulation of amino acid metabolism (and thus protein anabolism) in skeletal muscle. L-Glutamine and Exercise The intramuscular glutamine concentration is decreased in various catabolic conditions, including injury, surgery, uncontrolled diabetes, sepsis, burns, and prolonged, intensive exercise. Following an overnight fast, the plasma glutamine level normally ranges from 500 to 750 mmol/L. Evidence suggests there may be some value in using plasma glutamine as a blood marker for overtraining, immune system status, and other parameters in athletes, though the validity of such a technique requires further exploration. Conversely, anabolic growth factors such as IGF-I suppress glutamine release from skeletal muscle (Parry-Billings et al., 1993). In contrast to the reports of decreased plasma glutamine concentrations in overtrained athletes, elevations in plasma glutamine are observed in response to long-term balanced training. Whereas a reduction in the plasma glutamine level have been reported following endurance events and prolonged exercise. These levels remain unchanged or temporarily elevated after short-term, high-intensity exercise, though glutamine has been reported to fall in the recovery period following high-intensity intermittent exercise. Common factors among all of the aforementioned stress states are rises in the plasma concentrations of cortisol and glucagon and an increased tissue requirement for glutamine for gluconeogenesis. It is suggested that increased gluconeogenesis and associated increases in hepatic, gut and renal glutamine uptake account for the depletion of plasma glutamine in catabolic stress states, including prolonged exercise. The short term effects of exercise on the plasma glutamine level may be cumulative, since heavy training has been shown to result in low plasma glutamine levels (< 500 mumol/L) requiring long periods of recovery. Furthermore, athletes experiencing discomfort from the overtraining syndrome exhibit lower resting levels of plasma glutamine than active healthy controls. Therefore, physical activity directly affects the availability of glutamine to the leucocytes and thus may influence immune function. Since injury, infection, nutritional status and acute exercise can all influence plasma glutamine level, these factors must be controlled and/or taken into consideration if plasma glutamine is to prove a useful marker of impending overtraining. There is a high incidence of infections in athletes undergoing intense, prolonged training or participating in endurance races (e.g., the marathon), in particular, upper respiratory tract infections. Prolonged, exhaustive exercise can lower the plasma level of glutamine, reducing its availability as to serve as a fuel for immune cells and for its potential specific immunostimulatory effects. This could therefore be an important factor in the event of an impaired response of immune cells to opportunistic infections. The effects of feeding glutamine to sedentary individuals and to marathon and ultramarathon runners before and after prolonged, exhaustive exercise has been investigated in a series of studies that monitored the incidence of infections and some acute-phase response markers. Oral glutamine, compared with a placebo, appeared to have a beneficial effect on the incidence of infections reported by runners after a marathon. Plasma glutamine levels were decreased by approximately 20% 1 h after marathon running. A marked increase in numbers of white blood cells occurred immediately after exhaustive exercise, followed by a decrease in the numbers of lymphocytes. The provision of oral glutamine after exercise appeared to have a beneficial effect on the level of subsequent infections. In addition, the ratio of T-helper/T-suppressor cells appeared to be increased in samples from those who received glutamine, compared with placebo. Epidemiological data suggest that endurance athletes are at increased risk for upper respiratory tract infection during periods of heavy training and the 1- to 2-wk period following race events. There is growing evidence that, for several hours subsequent to heavy exertion, several components of both the innate (e.g., natural killer cell activity and neutrophil oxidative burst activity) and adaptive (e.g., T and B cell function) immune system exhibit suppressed function. At the same time, plasma pro- and anti-inflammatory cytokines are elevated, in particular interleukin-6- and interleukin-1-receptor antagonist. Various mechanisms explaining the altered immunity have been explored, including hormone-induced trafficking of immune cells and the direct influence of stress hormones, prostaglandin-E2, cytokines, and other factors. The immune response to heavy exertion is transient, and further research on the mechanisms underlying the immune response to prolonged and intensive endurance exercise is necessary before meaningful clinical applications can be drawn. Some attempts have been made through chemical or nutritional means (e.g., indomethacin, glutamine, vitamin C, and carbohydrate supplementation) to attenuate immune changes following intensive exercise. Whole-body glutamine appearance in plasma may amount to up to 60-100 g per day for a 70-kg man (Nurjhan et al., 1995); hence, in order to affect a change in muscle protein anabolism, it is expected that large, multi-gram quantities of glutamine will be required. REFERENCES Adegoke OA, McBurney MI, Samuels SE, Baracos VE (1999). Luminal amino acids acutely decrease intestinal mucosal protein synthesis and protease mRNA in piglets. J Nutr, 1219: 1871-1878. Ardawi MSM, Newsholme EA (1985). Fuel utilization in colonocytes of the rat. Biochem J, 231: 713. Bergstrom J, Furst P, Hultman E (1974). Intracellular free amino acid concentration in human muscle tissue. J Appl Physiol, 36: 693-697. Bowtell JL, Gelly K, Jackman ML, Patel A, Simeoni M, Rennie MJ (1999). Effect of oral glutamine on whole body carbohydrate storage during recovery from exhaustive exercise. J Appl Physiol, 86: 1770. Bulus N, Cersosimo E, Ghishan F, Abumrad NN (1989). Physiologic importance of glutamine. Metabolism, 38: 1. Cersosimo E, Williams PE, Radosevich PM, Hoxworth BT, Lacy WW, Abumrad NN (1986). Role of glutamine in adaptations in nitrogen metabolism during fasting. Am J Physiol, 250: E622-E628. Chopra IJ (1986). Nature, sources, and relative biologic significance of thyroid circulating hormones. In: Ingbar SH, Braverman LE, eds. Werners The Thyroid. A Fundamental and Clinical Text. Fifth Edition. Philadelphia: JB Lippincott. pp. 136-153. Danforth E Jr (1986). Effects of fasting and altered nutrition on thyroid hormone metabolism in man. In: Hennemann G, ed. Thyroid Hormone Metabolism. New York: Marcel Dekker Inc. pp. 335-358. Dent CE, Schilling JA (1949). Studies on the absorption of proteins: The amino acid pattern in portal blood. Biochem J, 44: 318. De Jong M, Docter R, Bernard BF, van der Heijden JT, van Toor H, Krenning EP, Hennemann G (1994). T4 uptake into the perfused rat liver and liver T4 uptake in humans are inhibited by fructose. Am J Physiol, 266: E678. de Vasconcelos MI, Tirapegui J (1998). Nutritional importance of glutamine. Arq Gastronenterol, 35: 207. Due P-H, Darcy-Vrillon B, Blachier F, Morel M-T (1995). Fuel selection in intestinal cells. Proc Nutr Soc, 54: 83. Egami MI, Guimaraes ARP, Nascimento Curi CMPO, Curi R (1993). Effect of fatty acids-rich dietes on thymocyte proliferation and thymus involution during growing. Physiol Behav, 53: 531. Engler D, Burger A (1984). The deiodination of the iodothyronines and their derivatives in man. Endocrine Rev, 5: 151. Fery F, Bourdoux P, Christophe J, Balasse EO (1982). Hormonal and metabolic changes induced by an isocaloric isoproteinic ketogenic diet in healthy subjects. Diabete Metab, 8: 299. Furst P, Albers S, Stehle P (1989). Evidence for a nutritional need for glutamine in catabolic patients. Kidney Int Suppl, 27: S287. Gavin LA, McMahon FA, Moeller M (1981). Carbohydrate in contrast to protein feeding increases the hepatic content of active thyroxine 5-deiodinase in the rat. Endocrinology, 109: 530. Hammarqvist F, Luo JL, Cotgreave IA, Andersson K, Wernerman J (1997). Skeletal muscle glutathione is depleted in critically ill patients. Crit Care Med, 25: 78. Hankard RG, Darmaun D, Sagar BK, D,more D, Parsons WR, Haymond MW (1995). Response of glutamine metabolism to exogenous glutamine in humans. Am J Physiol, 269: E663-E670. Hankard RG, Haymond MW, Darmaun D (1996). Effect of glutamine on leucine metabolism in humans. Am J Physiol, 271: E748. Haussinger D, Sies H, Gerok W (1985). Functional hepatocyte heterogeneity in ammonia metabolism. The intercellular glutamine cycle. J Hepatol, 1: 3. Herskowitz K, Bode BP, Block ER, Souba WW (1991). Characterization of L-glutamine transport by pulmonary endothelial cells. Am J Physiol, 260: L241. Hickson RC, Czerwinski SM, Wegrzyn LE (1995). Glutamine prevents down regulation of myosin heavy chain synthesis and muscle atrophy from glucocorticoids. Am J Physiol, 268: E730. Iiboshi Y, Kawasome H, Papst PJ, Terada N (1999). Amino-acid dependent control of p70S6k; addition of a single amino acid activates p70S6k. Abstract. J Paren Enter Nutr, 23: S148. Jepson MM, Bates PC, Broadbent P, Pell JM, Millward DJ (1988). Relationship between glutamine concentration and protein synthesis in rat skeletal muscle. Am J Physiol, 255: E166-E172. Kuhn KS, Schuhmann K, Stehle P, Darmaun D, Furst P (1999). Determination of glutamine in muscle protein facilitates accurate assessment of proteolysis and de novo synthesis-derived endogenous glutamine production. Am J Clin Nutr, 70: 484-489. Lavoinne A, Husson A, Quillard M (1998). Glutamine and the liver cell: metabolism, properties and the concept of metabolic regulation by cell swelling. Ann Biol Clin (Paris), 56: 557. Low SY, Rennie MJ, Taylor PM (1996a). Altered glycogen synthesis associated with changes in cell volume of rat skeletal muscle myotubes in primary culture. Biochem Soc Trans, 24: 244S. Low SY, Taylor PM, Rennie MJ (1996b). Responses of glutamine transport in cultured rat skeletal muscle to osmotically induced changes in cell volume. J Physiol, 492: 877. Meynial-Denis D, Mignon M, Miri A, Imbert J, Aurousseau E, Taillandier D, Attaix D, Arnai M, Grizard J (1996). Glutamine synthetase induction by glucocorticoids is preserved in skeletal muscle of aged rats. Am J Physiol, 271: E1061-E1066. Mittendorfer B, Volpi E, Wolfe RR (1998). Glutamine transport across skeletal muscle cells is impaired during aging. Abstract. Clin Nutr, 17: 32P. Neame KD, Wiseman G (1957). The transamination of glutamic and aspartic acids during absorption by the small intestine of the dog in vivo. J Physiol, 135: 442. Newsholme EA, Parry-Billings M (1990). Properties of glutamine release from muscle and its importance for the immune system. J Parent Enter Nutr, 14: 63S. Nurjhan N, Bucci A, Periello G et al. (1995). Glutamine: a major gluconeogenic precursor and vehicle for interorgan carbon transport in man. J Clin Invest, 95: 272. Olde Damink SW, de Blaauw I, Deutz NE, Soeters PB (1999). Effects in vivo of decreased plasma and intracellular muscle glutamine concentration on whole-body and hindquarter protein kinetics in rats. Clin Sci, 96: 639. Pacitti AJ, Austgen TR, Souba WW (1992). Mechanisms of increased hepatic glutamine uptake in the endotoxin-treated rat. J Surg Res, 53: 298. Parker PJ, Randle PJ (1978). Partial purification and properties of branched-chain 2-oxoacid dehydrogenase. Biochem J, 171: 751-757. Parry-Billings M, Bevan SJ, Opara E, Liu CT, Dunger DB, Newsholme EA (1993). The effects of growth hormone and insulin-like growth factors I and II on glutamine metabolism by skeletal muscle of the rat in vitro. Horm Metab Res, 25: 243. Plumley DA, Austgen TR, Salloum RM, Souba WW (1990). Role of the lungs in maintaining amino acid homeostasis. J Parenter Enter Nutr, 14: 569. Salloum RM, Souba WW, Fernandez A, Stevens BR (1990). Dietary modulation of small intestinal glutamine transport in intestinal brush border membrane vesicles of rats. J Surg Res, 48: 635. Sato T, Maruyama S, Saida K, Takata I (1982). Correlation of hepatic thyroxine 5' monodeiodination with hexose monophosphate shunt in young rats. Pediatr Res, 16: 377. Simon O (1989). Metabolism of proteins and amino acidss. In: Protein Metabolism in Farm Animals. Bock H-D, Eggum BO, Low AG, Simon O, Zebrowska T, eds. Berlin and Oxford: VEB Deutscher Landwirtschaftsverlag and Oxford University Press. pp. 273-366. Stumvoll M, Perriello G, Meyer C, Gerich J (1999). Role for glutamine in human carbohydrate metabolism in kidney and other tissues. Kidney Int, 55: 778. Souba WW (1987). Interogan ammonia metabolism in health and disease: A surgeons view. J Parent Enter Nutr, 11: 569. Tadros LB, Taylor PM, Willhoft NM, Rennie MJ (1993). Effects of glutamine deprivation on glutamine transport and synthesis in primary culture of rat skeletal muscle. Am J Physiol, 265: E935. Tietz NW (1990). Clinical Guide to Laboratory Tests. Philadelphia: Saunders. p. 262. van Acker BAC, von Meyenfeldt MF, van der Hulst RRWJ, Hulsewe KWE, Wagenmakers AJM, Deutz NEP, de Blaauw I, Dejong CH, van Kreel BK, Soeters PB (1999). Glutamine: The pivot of our nitrogen economy? J Parent Enter Nutr, 23: S45. Varnier M, Leese GP, Rennie MJ (1995). Stimulatory effect of glutamine on glycogen accumulation in human skeletal muscle. Am J Physiol, 269: E309. Watford M (1993). Hepatic glutaminase expression: relationship to kidney-type glutaminase and to the urea cycle. FASEB J, 7: 1468. Windmueller HG, Spaeth AE (1975). Intestinal metabolism of glutamine and glutamate from the lumen as compared to glutamine from the blood. Arch Biophys Biochem, 171: 662. Windmueller HG, Spaeth AE (1978). Identification of ketone bodies and glutamine as the major respiratory fuels in vivo for postabsorptive rat small intestine. J Biol Chem, 253: 69. Wiseman G (1953). Absorption of amino acids using an in vitro technique. J Physiol, 120: 63. Suggested Doses Take 5-20 grams daily in divided doses. Whole-body glutamine appearance in plasma may amount to up to 60-100 g per day for a 70-kg man (Nurjhan et al., 1995). Thus, to produce a noticeable effect, a multi-gram dose of glutamine is expected to be required. In healthy subjects consuming 5-10 grams of glutamine post-exercise, both liver and muscle glycogen resynthesis may be accelerated (Bowtell et al., 1999), thereby assisting in recovery from training and sparing endogenous (e.g., intramuscular) glutamine. Safety Issues These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure or prevent any disease.[/list:u:b7a0df736f] Quelle: http://www.kilosports.com/productdesc.cfm?ProductName=Glutamine%20Peptides Over & out, MVF

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Mario V. Fringes

Beiträge: 845
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Registriert: 29.05.2001

17.03.2003 12:55     Profil von Mario V. Fringes   Mario V. Fringes eine Nachricht schreiben     Beitrag editieren/löschen
Sup! Wollte fairerweise, da ich ja einen Pro-Glutamin Artikel gepostet habe, noch einen Artikel posten, in welchem sich der Autor eher negativ zu Glutamin äußert: [url=http://www.t-mag.com/nation_articles/body_230glut.html]Glutamine - Destroying the Dogma, Part 1[/url] BTW, 6 kg sind weg. Gruß, [i:7d686f62b8]Mario[/i:7d686f62b8] PPE CS

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Metalhead

Beiträge: 355
Aus: bielefeld
Registriert: 10.08.2002

25.03.2003 20:57     Profil von Metalhead   Metalhead eine Nachricht schreiben     Beitrag editieren/löschen
Nichts gegen Dich, aber von US Product Line gibt es auch reines Glutaminpeptid (schmeckt schon abartig bitter...) 400g für weniger als 20 Euro. Kommt also aufs gleiche raus. Was ist an Deinem denn besser? gruß

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Mario V. Fringes

Beiträge: 845
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25.03.2003 21:05     Profil von Mario V. Fringes   Mario V. Fringes eine Nachricht schreiben     Beitrag editieren/löschen
Metalhead, Glutaminpeptdid bleibt Glutaminpeptid! Wenn das Produkt von US Product Line günstiger zu haben ist, dann würde ich auch dieses Produkt kaufen. So einfach ist das! Gruß, Mario PPE CS

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Dragonknight

Beiträge: 72
Aus: Böblingen
Registriert: 03.03.2003

07.04.2003 08:25     Profil von Dragonknight   Dragonknight eine Nachricht schreiben     Beitrag editieren/löschen
@ Mario ich nehm mal an bis ich geschaltet hab ist schon alles weg oder? @ Metalhead wo hast du das Zeug denn gefunden?

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Mario V. Fringes

Beiträge: 845
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Registriert: 29.05.2001

09.04.2003 10:43     Profil von Mario V. Fringes   Mario V. Fringes eine Nachricht schreiben     Beitrag editieren/löschen
[quote:df2beae62f]@ Mario ich nehm mal an bis ich geschaltet hab ist schon alles weg oder?[/quote:df2beae62f] Dragonknight, sorry, hatte ganz vergessen diesen Thread zu updaten. Das Glutamin war schon nach einer Woche ausverkauft. Aber vielleicht kann Metalhead ja einen Link zum dem von ihm genannten Anbieter posten!? Gruß, [i:df2beae62f]Mario V. Fringes[/i:df2beae62f] Editor, Physique & Performance Engineering [b:df2beae62f] + + + Advertisement + + +[/b:df2beae62f] [url=http://www.physique-performance-engineering.com/]PPE - You can train or you can train intelligently. The choice is yours![/url]

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camus

Beiträge: 50
Aus:
Registriert: 07.06.2003

02.07.2003 11:07     Profil von camus   camus eine Nachricht schreiben     Beitrag editieren/löschen
hi jungs, eine frage neben bei ich habe was über Glutamin gelesen: " Achten Sie darauf, ausschließlich L-Glutamin als Glutaminquelle auszuwählen. Normale Glutaminsäure hilft hier wenig und L-Glutaminpeptid besteht leider nur zu einem Drittel aus L-Glutamin, was bedeutet, dass bei letzterer Form eine enorm hohe Tagesdosierung (mindestens 60 g) konsumiert werden müsste." was haltet ihr davon????? :shock:

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Some One

Beiträge: 998
Aus: Wien
Registriert: 15.03.2003

09.10.2003 10:49     Profil von Some One   Some One eine Nachricht schreiben     Beitrag editieren/löschen
Würde mich auch interessieren, denn ich hab auch ne Dose Glutaminpeptide zu Hause. Von Multipower :/

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