Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT02079 (lysine)
 58,762 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

18 free amino-acids have been valuated in a group of patients recovering from myocardial infarction dating more than one year back and in another group of healthy active athlets. In the group of the ill persons the mean values of the following amino-acids were significantly higher: Arginine, asparagine-acid, phenylalanine, valine, lysine, serine, threonine, leucine, proline and tyrosine. While in the group of the healthy persons the following amino - acids proved to have significantly higher values: alpha -- aminobutter-acid, glycine and cystine. No significant differences between the mean values of both groups were to be found of the following amino - acids: Alanine, methionine, ornithine, isoleucine and histidine. In the group of the patients correlations of the free amino acids to both serumlipids and blood -- glucose could be calculated with significant results in a certain number of amino-acids. The results may suppose that the changes in the metabolism of atherosclerotic patients do not only effect the lipids and carbohydrates, but as well the free amino-acids.
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PMID:[Free amino-acids of the plasma in atherosclerotic patients (author's transl)]. 1 52

Sepsis is a major catabolic insult resulting in modifications in carbohydrate and fat energy metabolism, and leading to increased muscle breakdown and nitrogen loss. Insulin resistance, which develops in sepsis, decreases glucose utilization, but plasma insulin levels are sufficiently elevated to prevent lipolysis, resulting in a further energy deficit. The availability of fuels in sepsis is therefore limited, and the body resorts to muscle breakdown, gluconeogenesis, and amino acid oxidation for energy supply. Previous work has not defined, however, the exact alterations in amino acid metabolism. Therefore, the following studies were undertaken. Blood samples were drawn from fifteen patients in whom the diagnosis of sepsis was clinically established; the samples were analyzed for amino acid, beta-hydroxyphenylethanolamines, glucose, insulin and glucagon concentrations. The plasma amino acid pattern observed was characterized by an increase in total amino acid content, due mainly to high levels of the aromatic amino acids (phenylalanine and tyrosine) and the sulfur-containing amino acids (taurine, cystine and methionine). Alanine, aspartic acid, glutamic acid and proline were also elevated, but to a lesser degree. The branched chain amino acids (valine, leucine and isoleucine) were within normal limits, as were glycine, serine, threonine, lysine, histidine and tryptophan. Those patients who did not survive sepsis had higher levels of aromatic and sulfur-containing amino acids as compared to those patients surviving sepsis. On the other hand, those patients surviving sepsis had higher levels of alanine and the branched chain amino acids. In a second group of five patients with overwhelming sepsis accompanied by a state of metabolic encephalopathy, a parenteral nutrition solution consisting of 23% dextrose, and an amino acid formulation enriched with branched chain amino acids was administered. In these five patients, normalization of the plasma amino acid pattern and reversal of encephalopathy was observed. The following sequence of events may be postulated: The septic patient develops insulin resistance in the peripheral tissues, primarily muscle, while the adipose tissue is much less affected. The insulin resistance and the inability to utilize fat leads to increased muscle proteolysis. Muscle breakdown results in release into the blood of enormous amounts of various amino acids; the muscle itself is able to oxidize the branched chain amino acids, supplying the muscles' own energy requirements and alanine for gluconeogenesis. The extensive muscle proteolysis coupled with relative hepatic insufficiency occurring early in sepsis results in the appearance in the plasma of high levels of most of the amino acids present in muscle, particularly the aromatic and the sulfur-containing amino acids. The outcome of patients with sepsis might be positively affected by combined therapy with glucose, insulin and branched chain amino acids.
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PMID:Amino acid derangements in patients with sepsis: treatment with branched chain amino acid rich infusions. 9 98

We described previously the existence of a soluble ATPase activity in rat liver mitochondria [1]. The purification and catalytic properties have been described [2]. In a continuation of these experiments, we have studied the immunologic and structural properties of one molecular form of this enzyme : ATPase I. We have prepared the antiserum anti-ATPase I and demonstrated the purity of our enzyme preparation by immunodiffusion and immunoelectrophoresis. An immunohistochemical method also confirmed the localization of ATPase I in the soluble fraction of mitochondria. The molecular weight of ATPase I was measured by G 100 Sephadex gel filtration and was found to be 18,400; electrophoresis on polyacrylamide gels gave a value of 18,600. The pHi of ATPase I was found to be 7,2. Amino acid analysis showed high amounts of aspartic acid, glutamic acid, serine and glycine. The molecular weight calculated from the total amino acid residues was found to be 17,000. Alanine is the NH2 terminal amino acid. The peptide maps obtained after degrading ATPase I with cyanogen bromide or trypsin are in accordance with the methionine, lysine and arginine residues we found in the ATPase I molecule. ATPase I does not appear to be a glycoprotein.
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PMID:Studies of soluble rat liver mitochondrial acid ATPases. II. Structural and immunological properties of ATPase 1. 15 69

Rat fibrinogen was purified from rat plasma by using lysine-Sepharose chromatography, repeated precipitation with 25%-satd. (NH(4))(2)SO(4) and gel chromatography on Sepharose 6B. To minimize proteolytic activity, rats were injected intravenously with Trasylol before bleeding and the collected blood was treated with Trasylol and di-isopropyl phosphorofluoridate. A 95%-clottable preparation was obtained in 70-75% yield; it proved to be free of factor XIII and plasminogen. It showed a single band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and on disc electrophoresis in 8m-urea. Alanine was the only detectable N-terminal amino acid. After reduction and modification of the thiol groups, the material could be separated into three distinct chains (Aalpha, Bbeta and gamma) by pore-limit polyacrylamide slab-gel electrophoresis in the presence of sodium dodecyl sulphate. The amino acid compositions of the whole fibrinogen and of the separated modified chains were determined. The molecular weights were 61000, 58000 and 51000 for Aalpha-, Bbeta- and gamma-chains respectively. Our results for the chains are in contrast with previous reports on rat fibrinogen [Bouma & Fuller (1975) J. Biol. Chem.250, 4678-4683; Stemberger & Jilek (1976) Thromb. Res.9, 657-660], in which no separation between Aalpha- and Bbeta-chains was achieved on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis for 3h. Evidence is presented that this is probably due to Aalpha-chain degradation as a result of incomplete inhibition of proteolytic enzymes during the purification. Complete inhibition of proteolytic activities is essential in all steps of the present purification procedure.
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PMID:Purification of rat fibrinogen and its constituent chains. 41 20

The free amino acids in eccrine sweat collected from the forearms of 20 healthy trained and 20 healthy untrained men during controlled exercise were determined quantitatively using ion exchange column chromatography. Sweat was deproteinized by adding an equal volume of 5% sulphosalicylic acid. The amino acid concentrations showed a constant qualitative pattern in sweat and large individual differences. Essential amino acids, such as isoleucine, leucine, lysine, methionine, phenylalanine, and valine were excreted in relatively small amounts. As compared to the trained men, untrained men showed statistically significantly higher concentrations in sweat for the following amino acids: Alanine, arginine, glycine, histidine, isoleucine, leucine, lysine, ornithine, phenylalanine, serine, taurine, threonine, tyrosine, and valine. No significant differences were found for citrulline, cystine, ethanolamine, and methionine. The comparison of the amino acid excretions in sweat obtained under controlled exercise and in urine showed that the amounts of amino acids excreted in sweat under controlled exercise were comparable to the losses of amino acids in urine.
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PMID:Quantitative study of free amino acids in human eccrine sweat excreted from the forearms of healthy trained and untrained men during exercise. 53 94

One hundred and sixteen freshly isolated rumen bacteria and 10 laboratory strains were studied for the production and excretion of free amino acids during growth in a basal medium containing glucose, cellobiose, and soluble starch as the energy sources, (NH4)2SO4 as the prime nitrogen source, volatile fatty acids, hemin, vitamins, Na2CO3, and cysteine as the reducing agent. Amino acid analyses of 48-h culture fluids of the isolates indicated the presence of alanine, glutamic acid, valine, aspartic acid, glycine, serine, lysine, methionine, leucine, isoleucine, threonine, histidine, arginine, phenylalanine, and tyrosine. Most isolates excreted some free amino acids. Alanine, glutamic acid, valine, aspartic acid, and glycine were found in the greatest concentrations with some isolates accumulating between 50 and 295 microgram/ml of one or more of these compounds. Concentrations of the remaining amino acids rarely exceeded 20 microgram/ml of culture fluid. Growth studies demonstrated that the amino acids were excreted during active growth of the bacteria and ceased shortly after growth became limited.
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PMID:The production of extracellular amino acids by rumen bacteria. 72 52

The specificity of amino acid transport in normal (high-glutathione) sheep erythrocytes was investigated by studying the interaction of various neutral and dibasic amino acids in both competition and exchange experiments. Apparent Ki values were obtained for amino acids as inhibitors of L-alanine influx. Amino acids previously found to be transported by high-glutathione cells at fast rates (L-cysteine, L-alpha-amino-n-butyrate) were the most effective inhibitors. D-Alanine and D-alpha-amino-n-butyrate were without effect. Of the remaining amino acids studied, only L-norvaline, L-valine, L-norleucine, L-serine and L-2,4-diamino-n-butyrate significantly inhibited L-alanine uptake. L-Alanine efflux from pre-loaded cells was markedly stimulated by extracellular L-alanine. Those amino acids that inhibited L-alanine influx also stimulated L-alanine efflux. In addition, D-alanine, D-alpha-amino-n-biutyrate, L-threonine, L-asparagine, L-alpha, beta-diaminoproprionate, L-ornithine, L-lysine and S-2-aminoethyl-L-cysteine also significantly stimulated L-alanine efflux. L-Lysine uptake was inhibited by L-alanine but not by D-alanine, and the inhibitory potency of L-alanine was not influenced by the replacement of Na+ in the incubation medium with choline. L-Lysine efflux from pre-loaded cells was stimulated by L-alanine but not by D-alanine. It is concluded that these cells possess a highly selective stero-specific amino acid-transport system. Although the optimum substrates are small neutral amino acids, this system also has a significant affinity for dibasic amino acids.
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PMID:Substrate specificity of amino acid transport in sheep erythrocytes. 84 80

Plasma amino acid concentrations were determined in virgin female rats, in pregnant rats (12 and 21 days after impregnation) and in 21-day foetuses. The total amino acid concentration in plasma decreases significantly with pregnancy, being lower at 12 than at 21 days. Alanine, glutamine+glutamate and other 'gluconeogenic' amino acids decrease dramatically by mid-term, but regain their original concentrations at the end of the pregnancy. With most other amino acids, mainly the essential ones, the trend is towards lower concentrations which are maintained throughout pregnancy. These data agree with known nitrogen-conservation schemes in pregnancy and with the important demands on amino acids provoked by foetal growth. In the 21-day foetuses, concentrations of individual amino acids are considerably higher than in their mothers, with high plasma foetal/maternal concentration ratios, especially for lysine, phenylalanine and hydroxy-proline, suggesting active protein biosynthesis and turnover. All other amino acids also have high concentration ratios, presumably owing to their requirement by the foetuses for growth. Alanine, glutamine+glutamate, asparagine+aspartate, glycine, serine and threonine form a lower proportion of the total amino acids in foetuses than in the virgin controls or pregnant rats, probably owing to their role primarily in energy metabolism in the adults. The results indicate that at this phase of foetal growth, the placental amino acid uptake is considerable and seems to be higher than immediately before birth.
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PMID:Plasma amino acid concentrations in pregnant rats and in 21-day foetuses. 90 17

Arterial blood concentrations of insulin, glucagon, and various substrates were determined in six anephric subjects in the postabsorptive state and immediately after hemodialysis. Plasma glucose and serum insulin concentrations were normal, and declined during dialysis. Plasma glucagon was elevated and remained unchanged. There was moderate hypertriglyceridemia before dialysis, but this decreased significantly after administration of heparin just before the start of dialysis, and at the end of dialysis was lowered further into the normal range. Comparison of postabsorptive whole blood concentrations of amino acids with those in normal, healthy adults revealed striking differences. Glutamine, proline, citrulline, glycine and both 1- and 3-methyl-histidines were increased, while serine, glutamate, tyrosine, lysine, and branched-chain amino acids were decreased. The glycine/serine ratio was elevated to 300% and tyrosine/phenylalanine ratio was lowered to 60% of normal. To investigate the potential role of blood cells in amino acid transport, the distribution of individual amino acids in plasma and blood cell compartments was studied. Despite a markedly diminished blood cell mass (mean hematocrit, 20.6 +/- 1.4%), there was no significant decrease in the fraction of most amino acids present in the cell compartment, and this was explained by increases of several amino acids in cellular water. None were decreased. Furthermore, during dialysis, whole blood and plasma amino acids declined by approximately 30% and 40%, respectively, whereas no significant change was observed in the cell compartment. Alanine was the only amino acid whose concentration declined in the cells as well as in plasma. The results indicate (a) significant alterations in the concentrations of hormones and substrates in patients on chronic, intermittent hemodialysis; (b) removal of amino acids during hemodialysis, predominantly from the plasma compartment, with no significant change in cell content; and (c) a redistribution of amino acids in plasma and blood cell compartments with increased gradients of most of the amino acids per unit cell water, by mechanism(s) as yet undetermined.
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PMID:Hormone-fuel concentrations in anephric subjects. Effect of hemodialysis (with special reference to amino acids). 93 88

Experiments were conducted to investigate plasma free amino acid concentrations in the chick. After one hour of fasting, total plasma amino acid concentration decreased to approximately half of the full-fed value. Within three to six hours, most amino acids had returned toward the full-fed level but did not exceed it throughout a 48 hour period of starvation. However, after 48 hours fasting lysine, threonine, and isoleucine accumulated three-fold, two-fold and two-fold of the full-fed level, respectively. Serine and glutamic acid exceeded the full-fed level at three hours and then declined. Alanine reached its highest level after six hours of fasting and then declined. In full-fed chicks diurnal variations of plasma free amino acid concentrations were observed. The lowest and highest concentrations were observed at 11 a.m. and 8 to 11 p.m., respectively under a 24 hr-lighting. Reference plasma amino acid patterns are reported for chicks fed a practical diet ad libitum. In day-old chicks, concentrations of total amino acids, methionine plus one half cystine, lysine, and arginine were high. Alanine and glutamic acid concentrations were low. Most amino acid concentrations declined gradually during the first four weeks of life, but methionine plus one half cystine, phenylalaine, threonine and serine concentrations decreased sharply between two and four weeks. Lysine concentration continued to decrease in chicks fed the starter diet. At 20 weeks, plasma amino acid concentrations had decreased considerably except for methionine plus one half cystine and basic amino acids. The plasma amino acid pattern for chicks fed an isolated soybean protein diet was similar to that of chicks fed the practical diet.
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PMID:Conditions affecting plasma amino acid patterns in chickens fed practical and purified diets. 103 38


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