Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.6.1.2 (alanine aminotransferase)
26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

After borohydride reduction, carboxymethylation, and tryptic digestion of the holoenzyme of pig heart alanine aminotransferase, a single icosapeptide containing the N6-(phosphopyridoxyl)lysine residue was isolated by a combination of gel filtration and ion-exchange chromatogrpahy. Its primary structure was determined as Gln-Glu-Leu-Ala-Ser-Phe-His-Ser-Val-Ser-Lsy(Pxy)-Gly-Phe-Met-Gly-Glu-Cys-Gly-Phe-Arg.
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PMID:Pyridoxal 5'-phosphate binding site of pig heart alanine aminotransferase. 46 50

Changes in serum amino acid levels and time course of hepatic function derangements were studied in mongrel dogs with choledochus ligature and subsequent biliarly reconstruction through cholecysto-duodenostomy. In the second week after choledochus ligature, serum ammonium level increased along with intensification of jaundice. After four weeks, GPT activity was higher than GOT and plasma albumin level markedly decreased with similar reduction in serum amino acid levels. Biliary reconstruction, when performed during three or four weeks after the ligature, restored the hepatic function as well as serum amino acid levels toward normal. When it was performed in the fifth or sixth week after the ligation, the liver function did not restore and serum levels of total amino acids, essential and non-essential amino acids increased even 4 weeks lapse after reconstruction. Among the changes observed, His., Val., Ser., Arg., Leu., Ileu, Phe, and Lys. were increased, whereas Pro. and Cys. disappeared from the serum. These results suggest that recovery from metabolic changes of amino acids due to choledochus ligature depends upon the duration of obstructive jaundice, i.e., it appears necessary to perform the biliary reconstruction within four weeks after the initiation of obstruction.
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PMID:[Experimental study on changes in serum amino acid levels following choledochus ligature and subsequent biliary reconstruction (author's transl)]. 82 88

Protein hydrolysate-containing parenteral solutions have been reported to be hepatotoxic. Ten infants who were treated with a 20 percent glucose solution containing either 2.5 percent or 3.25 percent protein hydrolysate are reviewed. Their gestational ages were 30 to 40 weeks and births weights 1000 to 35000 g. Serum glutamate-oxaloacetate transaminase (GOT), glutamate-pyruvate transaminase (GPT), leucine amino peptidase (LAP) and bilirubin were measured serially. Serum amino acids were measured and consistently demonstrated decreased levels of isoleucine and increased aspartic acid, glutamic acid, serine, proline, glycine, alanine, threonine and lysine. The amino acid imbalances were associated with transaminase elevations in eight infants. Serum bilirubin levels increased in six patients and LAP in four. Liver biopsies from three patients showed minimal to moderate hepatic parenchymal disease with cholestasis.
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PMID:The hepatotoxicity of parenteral protein hydrolysate-containing solutions. 82 62

Isolated rat livers were perfused for 6 hours by different types of cell-free synthetic media. Some of the media included perfluoro-compounds as an oxygen carrier. The value of the perfusion medium as blood substitute was judged on the basis of observations and measurements of a number of parameters. These were: secretion of bile, fluid pressure in the portal vein, the level of GPT (ALAT) transaminase, urea nitrogen, and glucose in the perfusate. The rate of albumin synthesis and the rate of 14-C-lysine incorporated into circulating proteins were also measured. It was found that perfusion of the isolated rat liver with the TC-199 Difco medium containing the perfluoro-compound FC-80 emulsion maintained the liver in a good condition demonstrated, among other things, by the synthesis of albumin and other proteins. The liver could be kept in a good functional condition during 6 hours perfusion with this cell-free medium. With all the other types of perfusate tested the liver did not synthesize proteins. The isolated rat liver seems to be both convenient and advantageous for testing the perfusion media with respect to their capacity to maintain important metabolic functions.
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PMID:Studies on isolated rat liver perfused by perfluoro-compound emulsion. 112 46

L-Leucine-pyruvate transaminase obtained from Acetobacter suboxydans exhibited absorbance maxima to 280 and 332 nm. The 332 nm peak was derived from the coenzyme bound to the enzyme protein with the epsilon NH2 of a lysine residue. The transaminase showed reactivity against many L-amino acids. The relation between the reactivity and the structure of the amino donor is discussed. The Michaelis constants for L-leucine, pyruvate, L-alanine and alpha-ketoisocaproate were 6.7, 3.1, 7.1 and 0.9 mM, respectively. The equilibrium constant was 5.3. The activation energy at pH 5.0 was 8,800 cal/mol.
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PMID:Further characterization of L-leucine-pyruvate transaminase from Acetobacter suboxydans. 115 85

The synthesis and release of alanine and glutamine have been studied in the intact rat epitrochlaris skeletal muscle preparation. Aspartate, cysteine, leucine, valine, methionine, isoleucine, serine, theronine, and glycine increased significantly the formation and release of alanine from muscle. Cysteine, leucine, valine, methionine, isoleucine, tyrosine, lysine, and phenylalanine increased the rate of glutamine synthesis. Only ornithine, arginine, and tryptophan were without effect on the synthesis of either alanine or glutamine. Half-maximal stimulation of alanine and glutamine formation by added amino acids was observed with concentrations ranging between 0.5 and 1.0 mM. Increases in alanine and glutamine formation were not accompanied by changes in pyruvate production or glucose uptake. The progressive decline in alanine and glutamine synthesis noted on prolonged incubation was prevented by the addition of amino acids to the incubation medium. Stimulation of alanine synthesis by added amino acids was unaffected by inhibition of glycolysis with iodoacetate. Inhibition of alanine aminotransferase with aminooxyacetate significantly decreased alanine formation. Pyruvate and ammonium chloride did not increase further the rate of either alanine or glutamine formation above that produced by added amino acids. These data indicate that most amino acids are precursors for alanine and glutamine synthesis in skeletal muscle. A general mechanism is presented for the de novo formation of alanine from amino acids in skeletal muscle, and the importance of proteolysis for the supply of amino acid precursors for alanine and glutamine synthesis is discussed.
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PMID:Alanine and glutamine synthesis and release from skeletal muscle. II. The precursor role of amino acids in alanine and glutamine synthesis. 124 59

Response characteristics are presented for a dual-enzyme fiber-optic biosensor for glutamate. An enzyme layer composed of glutamate dehydrogenase (GDH) and glutamate-pyruvate transaminase (GPT) is used to produce reduced nicotinamide adenine dinucleotide (NADH) at the tip of a fiber-optic probe. NADH luminescence is monitored through this probe and the measured fluorescence intensity is related to the concentration of glutamate. GDH catalyzes the formation of NADH, and GPT drives the GDH reaction by removing a reaction product and regenerating glutamate. Optimal response is obtained in a pH 7.4 Tris-HCl buffer maintained at 25 degrees C in the presence of 4 mM NAD+ and 10 mM L-alanine. The temperature profile reveals a strong negative temperature effect which is attributed to the temperature dependency of NADH luminescence. Under optimal conditions, the sensor sensitivity is 0.127 nA/microM over the 1-10 microM concentration range, the detection limit is 0.13 microM, and response times range from 4 to 8 min. The sensor response is stable for 12 days when stored at 4 degrees C. Selectivity for glutamate is excellent over most of the common amino acids as well as ascorbic acid, uric acid, taurine, and GABA. Only slight responses were observed for glutamine and lysine. The effect of ammonia on the glutamate response was found to be minimal at total ammonia nitrogen concentrations as high as 200 microM.
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PMID:Dual-enzyme fiber-optic biosensor for glutamate based on reduced nicotinamide adenine dinucleotide luminescence. 135 Apr 33

Twenty-eight patients with suspected Reye's syndrome (RS) were seen in our Department from 1974 through 1987. Liver biopsy confirmed the diagnoses of RS and non-icteric fulminant hepatitis (NIFH) in 7 and 5 cases, respectively. NIFH was the most common RS mimicker. Total bilirubin, LDH and serum ammonia levels showed no significant differences between RS and NIFH. However, the levels of serum GOT and GPT were significantly higher in the NIFH group. Serum and urinary carnitine levels were measured in both groups, but the results were inconclusive. Amino acid analysis in one RS and two NIFH patients showed no significant differences in the ratio of branched chain to aromatic amino acids. However, one RS patient showed a high level of lysine. Histological findings in the liver of two NIFH patients showed minor mitochondrial swelling and microvesicular fat, but the major finding was hepatic necrosis. Our experience indicates that NIFH and RS cannot be differentiated by routine laboratory tests. Liver biopsy is essential for the accurate diagnosis of RS.
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PMID:Non-icteric fulminant hepatitis and Reye's syndrome: comparison of laboratory data. 228 22

In order to clone hepatitis C (blood-borne non-A, non-B hepatitis) virus, lambda gt11-cDNA library was constructed from RNA extracted from 100 liters serum collected from 1,047 donors with elevated ALT levels and negative for hepatitis B virus-DNA. The library was immunoscreened on Y1090 cells with pooled serum obtained from patients with acute hepatitis C or chronic hepatitis C. By screening 29 clones specific for Japanese hepatitis C infection were isolated. The specificity of these clones for hepatitis C infection was determined by panels constructed in 3 laboratories. Of these, 12 clones were specific for American hepatitis C infection as well. The nucleotide sequence (201 bp) of one of them was determined to be unique compared to known human viruses including hepatitis A virus, hepatitis B virus and hepatitis D virus. Southern blot analysis showed the absence of the sequence of the human genome in the clone. The predicted amino acid sequence is rich in residues of lysine, arginine, glutamic acid and asparagine, while lacking leucine, cysteine and methionine.
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PMID:Cloning of a cDNA associated with acute and chronic hepatitis C infection generated from patients serum RNA. 250 78

The effects of recombinant human interleukin-1 beta (rhIL-1 beta) on various serum constituents were studied following subcutaneous injection (12.5 or 125 micrograms/kg) in female Wistar rats. Protein electrophoresis and the determination of the serum concentrations of carboxypeptidase N (CPN), aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, aldolase, total proteins, iron, urea, creatinine, and several amino acids were performed 12, 24, and 72 hr after injection. With both doses of rhIL-1 beta, iron, albumin, CPN, and lysine were significantly decreased whereas alpha 2-globulin, urea, and creatinine were significantly increased 12 hr after administration. Iron and CPN were still low after 24 hr but returned to normal levels after 72 hr. With the higher dose of rhIL-1 beta, only alanine and phenylalanine levels were increased after 12 and 72 hr, taurine after 12 hr, and methionine after 24 hr. There were no biochemical or histological signs of hepatotoxicity. The findings indicate that rhIL-1 beta produces a reversible alteration of various biochemical plasma constituents without any apparent signs of cytotoxicity. Moreover, the decrease in CPN observed may influence the degradation of inflammatory peptides.
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PMID:Recombinant human interleukin-1 beta decreases serum carboxypeptidase N and modifies serum amino acid concentrations in rats. 278 29


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