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At least 343 records · Page 19Linked to original sources
PubMed2000

Acute intermittent porphyria associated with transient elevation of transaminases during an acute attack.

A 44-year-old woman with acute intermittent porphyria (AIP) was admitted to Kudanzaka Hospital because of abdominal pain. A cholecystectomy was performed in another hospital without improvement. On admission, her transaminases were elevated to greater than 1,000 mU/ml. After an intravenous drip of mainly glucose, her transaminases returned to normal. Her acute attacks occurred during stress, and she died of respiratory failure after repetitive acute episodes. AIP should be included in a list of the differential diagnosis of gastrointestinal diseases, neurosis, and hysteria. This is the first case of AIP accompanied by transient marked elevation of transaminases during an acute attack.

Adult↗
PubMed1985

Cholestasis in alcoholic chronic pancreatitis. Diagnostic value of the transaminase ratio for differentiation between extra- and intra-hepatic cholestasis.

In our long-term study of alcoholic chronic pancreatitis (median follow-up time, 10.4 years) 84 of 173 patients (48.6%) developed transient or persistent cholestasis with or without hyperbilirubinemia. We studied the discriminative value of the ASAT/ALAT ratio to differentiate intrahepatic (IHC) and extrahepatic cholestasis (EHC; due to stenosis of the distal common bile duct) in 75 of these patients. In 45 patients with persistent or recurrent cholestasis (group A) the cause of cholestasis was documented by accurate morphological methods. Thirty of the other 39 patients with transient cholestasis (group B) were classified on the basis of the overall clinical evaluation. Of 37 patients with IHC 36 had an ASAT/ALAT ratio of 1.5 or higher (one patient had normal values for both transaminases). Out of 38 patients classified as EHC 29 had an ASAT/ALAT ratio of 1.4 or lower (9 with normal transaminases being excluded). One patient with cholangitis secondary to EHC had a transient elevation of the ASAT/ALAT ratio to above 2.5. Thus our data suggest that in alcoholic chronic pancreatitis associated with cholestasis an ASAT/ALAT ratio of 1.4 or lower (or normal transaminases) usually indicates EHC. Diagnostic study and surgical decompression is mandatory in these cases if EHC persists.

Alanine Transaminase↗
PubMedDate not supplied

[Amino acid composition and transaminase activity in fish tissues, in a medium containing Cyanophyceae].

The content of free amino acids, activity of aspartate and alanine transaminase, number of sulphydryl groups in fish tissues were studied as affected by lethal amounts (3.2 g/l) of blue-green algae. Blue-green algae have a certain affect on fishes not only by excreting biologically active substances in the process of vital activity and decay but also changing the gas regime of the medium (the oxygen content lowers, the amount of carbon dioxide increases). Under the algae effect the total content of free amino acids in the fish liver, intestine and muscles increases, mainly due to a rise in the content of glutamic acid with threonine and aspartic acid with serine. These changes are most essential in the liver, intestine and are less pronounced in the muscles. Under the effect of blue-green algae the activity of aspartate transaminase increases in the heart, brain and decreases in the intestine. The activity of alanine transaminase enhances in the heart, intestine and brain. The ration value for these enzymes changes significantly in the brain, liver, intestine, but does not differ from the control in the muscles.

Alanine Transaminase↗
PubMed1975

Subcellular distribution and properties of rat liver kynurenine transaminase.

Kynurenine transaminase activity in rat liver was found in both the mitochondrial and supernatant fractions. The mitochondrial and supernatant fractions contained (a) kynurenine pyruvate transaminase which showed a preference for pyruvate as amino-acceptor and a pH optimum between 8.0 and 8.5 and (b) kynurenine alpha-ketoglutarate transaminase with a preference for alpha-ketoglutarate and a pH optimum between 6.0 and 6.5.

Animals↗
PubMed1990

[Preliminary studies on transaminase of Oncomelania snail].

By paper chromatography, the tissue homogenate of Oncomelania snails was shown to form glutamic acid at the expense of alpha-ketoglutarate plus aspartic acid, alanine or arginine respectively. The existence of alanine-glutamate, aspartate-glutamate and arginine-glutamate transaminase in Oncomelania snail was demonstrated. By using colorimetric method, the activity of aspartate-glutamate transaminase (GOT) and alanine-glutamate transaminase (GPT) of Oncomelania snail was 1.64 +/- 0.01 and 0.99 +/- 0.01 mumol/h.mg protein respectively. GOT and GPT were not inhibited by 2 ppm bromoacetamide, but the activity of GPT was suppressed (40%) by 2 ppm nicotinanilide. A combination of 0.5 ppm bromoacetamide and 0.5 ppm nicotinanilide had no synergitic molluscicidal effect.

Acetamides↗
PubMed1990

Sequential changes of serum transaminase and abdominal sonography in patients with suspected dengue fever.

Southern Taiwan experienced a dengue (type 1) outbreak in the autumn of 1988. One hundred and thirteen febrile patients suspected as having dengue infection were seen in the emergency room of the Kaohsiung Medical College Hospital. These patients were recruited for this study. Two hundred and eighty-six sequential serum aspartate transaminase (AST) and alanine transaminase (ALT) data from these patients were analyzed. Data analysis showed serum AST had increased daily and all data were out of normal range from day 6 of the illness. Compared to the AST level on the first day of the illness, the AST level was noted to elevate to an average of 9.25 folds on day 6. The sequential changes of AST were as follows: AST had elevated since the third ill-day in most cases and reached a peak on the 7th or 8th ill-day. It then declined gradually from the 8th ill-day and became normal about 3 weeks later. The changes of ALT level were about the same as AST but had later onset and lower peak. Abdominal sonographic examinations showed thickening of the gall bladder wall, splenomegaly and ascites in some patients during acute stage of the illness and recovered completely after patients recovered from the dengue attack. The sequential change of serum transaminase levels and sonographic findings were compatible. These findings may be used as a reference for the differential diagnosis among dengue fever, acute hepatitis and acute cholecystitis.

Abdomen↗
PubMed1986

Naltrexone hydrochloride (Trexan): a review of serum transaminase elevations at high dosage.

In summary, evidence is presented associating typically asymptomatic and reversible elevations of serum transaminase values with high daily dosages of naltrexone. Statistical significance was found only between placebo and the 300 mg dosage. Subjects aged 40 years and over were significantly more likely to develop this finding than younger subjects. All subjects with significant elevations of transaminase values in these studies took daily naltrexone dosages higher than recommended for opioid addiction. The daily dosage of naltrexone recommended for opioid addiction did not cause abnormalities of serum transaminase values in these studies.

Adult↗
PubMed1986

A purified cysteine conjugate beta-lyase from rat kidney cytosol. Requirement for an alpha-keto acid or an amino acid oxidase for activity and identity with soluble glutamine transaminase K.

Cysteine conjugate beta-lyase has been purified from rat kidney cytosol. The enzyme is a 100,000-dalton dimer of two 55,000-dalton subunits and has an absorption maximum at 432 nm. The enzyme has phenylalanine alpha-keto-gamma-methiolbutyrate transaminase activity and appears to be identical to rat kidney cytosolic glutamine transaminase K. Metabolism of S-1,2-dichlorovinyl-L-cysteine (DCVC) by the purified enzyme was dependent on the presence of either alpha-keto-gamma-methiolbutyrate or a protein factor which is present in the cytosolic fraction of rat kidney cortex. The protein factor was identified as a flavin containing L-amino acid oxidase which oxidized DCVC to S-(1,2-dichlorovinyl)-3-mercapto-2-oxopropionic acid. S-(1,2-Dichlorovinyl)-3-mercapto-2-oxopropionic acid has not been previously reported as a metabolite of DCVC. The data also show that rat kidney cytosolic glutamine transaminase K catalyzes both a beta-elimination and a transamination reaction with DCVC when alpha-keto-gamma-methiolbutyrate is present and that amino acid oxidase and alpha-keto-gamma-methiolbutyrate stimulate the enzyme activity by providing amino acceptors. When incubations were done with DCVC as substrate in the presence of excess alpha-keto-gamma-methiolbutyrate, the beta-lyase catalyzed beta-elimination and transamination in a ratio of 1:1.3, respectively. Under conditions where most of the alpha-keto-gamma-methiolbutyrate was consumed, the beta-elimination predominated indicating that the S-1,2-dichlorovinyl-3-mercapto-2-oxopropionic acid pool was consumed by transamination after the alpha-keto-gamma-methiolbutyrate had been depleted. The data are discussed with regard to the importance of these pathways as regulators or participants in the toxicity of S-cysteine conjugates.

Amino Acid Oxidoreductases↗
PubMedDate not supplied

[Topography, physicochemical and kinetic properties of the branched amino acid transaminases of the gastric and pancreatic mucosa].

About 40% of transaminase of branched amino acids were shown to be localized in mitochondrial matrix of pancreatic gland. The transaminases from pancreas and gastric mucosa had pH optima around pH 8.6. The enzymatic activity was increased with an increase in temperature to 50 degrees. In presence of 10 microM concentration of alpha-ketoglutarate Km volume of these two enzymes from postmitochondrial fraction of gastric mucosa and of pancreas were equal to 9.7 . 10(-4)M and 9.0 . 10(-4)M for leucine, 1.1.10(-4) M and 4.10(-3) M for valine, 6.4.10(-4) M and 8.5.10(-4) for isoleucine, respectively. The reaction or transamination proceeded via formation of a substituted form of the enzyme. The transaminase activity was inhibited by capronic acid (I506.8.10(-4) M), valeric acid (I508.10(-4)M), butyric acid (I50 5.8.10(-3) M) and propionic acid (I50 2.10(-2) M).

Amino Acids, Branched-Chain↗
PubMed1984

[Immunological indices of viral hepatitis patients and the prognosis for the time periods of aspartate and alanine transaminase normalization].

The work presents the results of the correlation analysis and the regression equation between the number of T-lymphocytes, the levels of IgA, IgM, IgG and the dynamics of the fall of the alanine and asparagine transaminase levels; the work also presents the results of the leukocyte migration inhibition test and the data on the duration of the presence of asparagine transaminase and alanine transaminase in the blood. The relationship between the normalization of enzymatic samples from the liver and the immune status in patients with viral hepatitis A and B is shown.

Alanine Transaminase↗
PubMedDate not supplied

[Alteration of activities of alanine- and aspartate transaminases in rat brain under conditions of hypothermia of various duration and in adrenalectomy].

Cooling of rats down to the rectal temperature of 20 degrees decreased the alanine- and aspartate transaminase activities in brain tissue. Activity of the enzymes studied was increased after prolongation of the hypothermia within 2 hrs. In adrenalectomized animals hypothermia was responsible for activation of aspartate transaminase and for a decrease in activity of alanine transaminase.

Adrenalectomy↗
PubMed1980

Studies on the kinetics and stoichiometry of inactivation of Pseudomonas omega-amino acid:pyruvate transaminase by gabaculine.

A homogeneous pyruvate-requiring omega-amino acid transaminase from Pseudomonas species F-126 has been examined for its behavior with gamma-aminobutyrate (GABA) as omega-amino acid substrate and for its susceptibility to the cyclic dihydroaromatic GABA analogue, gabaculine, a known suicide substrate for alpha-ketoglutarate-requiring GABA transaminases (Biochemistry 16, 4604-4610, 1977). One isomer of DL-gabaculine serves as a completely efficient titrant (no product molecules released) for this omega-amino acid transaminase by the anticipated mechanism of bound pyridoxal 5'-phosphate (PLP) derivitization. Stoichiometric titration with [2-3H]gabaculine reveals full inactivation at 0.45 labels/enzyme tetramer (see below), consistent with the subsequent demonstration that there is only 0.45 PLP molecule, bound as phenylhydrazine-titratable aldehyde form, per tetramer. Spectroscopic monitoring of inactivation also agrees with formation, on full inactivation, of 0.45 mol of m-anthranilyl-PNP adduct as the species quantitatively responsible for enzyme inactivation. Incubation of enzyme with excess PLP at 60 degrees C allows loading of enzyme with coenzyme to an average level of approximately 1 PLP/subunit, but even in this case activity is only increased up to 1.5-fold, and 1 to 1.5 molecules of gabaculine/tetramer cause complete inactivation. These data may indicate negative cooperativity between subunits.

Cyclohexanecarboxylic Acids↗
PubMed1980

Hepatic transaminase activity in alocholic liver disease.

Glutamic oxaloacetic transaminase (GOT) and glutamic pyruvic transaminase (GPT) activity were measured in precutaneous needle biopsy specimens of human liver tissue and compared with transaminase values in serum obtained on the day of biopsy. Hepatic GPT activity was significantly decreased in liver tissue of patients with alcoholic hepatitis and cirrhosis compared with the activity in individuals with normal livers (P less than 0.05) and individuals with primary biliary cirrhosis (P less than 0.05). The decreased hepatic GPT activity was not related to the presence of cirrhosis in biopsy specimens and was not increased by the addition of saturating amounts of pyridoxal phosphate to the assay mixture. Hepatic GOT was also slightly but significantly lowered in individuals with alcoholic liver disease (P less than 0.05). The GOT/GPT ratio in serum and liver tissue was increased only in individuals with alcoholic liver disease, but the increase did not reach statistical significance. The increased GOT/GPT ratio is due primarily to the low activity of GPT in liver and serum. The less than expected elevation of GPT in serum of patients with alcoholic hepatic reflects the diminished hepatic GPT activity and lesser amounts of this enzyme available to leak into serum from damaged hepatocytes.

Alanine Transaminase↗
PubMed1994

Selenomethionine as substrate for glutamine transaminase.

Selenomethionine is as a good substrate as methionine for bovine liver glutamine transaminase (E.C. 2.6.1.15). Almost identical Km values for methionine, selenomethionine, 4-methylthio-2-oxobutanoic acid and 4-methylseleno-2-oxobutanoic acid have been obtained. Like for other enzymes, also for glutamine transaminase the substitution of the sulfur atom in a substrate molecule by a selenium one does not appreciably affect the enzyme affinity. Glutamine transaminase may thus be involved in selenomethionine catabolism.

Animals↗
PubMed1977

Inactivation of bacterial D-amino acid transaminase by beta-chloro-D-alanine.

Purified D-amino acid transaminase from Bacillus sphaericus catalyzes an alpha,beta elimination from the D isomer of beta-chloroalanine to yield equivalent amounts of pyruvate, chloride, and ammonia; the L isomer of chloroalanine is not a substrate for this transaminase. During the beta elimination there is a synchronous loss in enzyme activity; the Kinact for beta-chloroalanine was estimated to be about 10 micrometers. The alpha-aminoacrylate-Schiff base intermediate formed after beta elimination of chloride ion is probably the key intermediate that partitions between one inactivation event for every 1500 turnovers. In the presence of D-alanine and alpha-ketoglutarate, which are good substrates for the transaminase activity of this enzyme, beta-chloroalanine is a potent, competitive inhibitor (K1 = 10 micrometers) with D-alanine and a weak, uncompetitive inhibitor with alpha-ketoglutarate.

Alanine↗
PubMed1996

[The prevalence of hepatitis C antibodies among volunteer blood donors with elevated blood transaminase and antibodies to the B virus core antigen].

The use of non-specific markers before 1989 (increased serum transaminase values and antibodies to hepatitis B core antigen) as a screening method for blood donors in an attempt to decrease the incidence of post-transfusional non-A non-B hepatitis (currently hepatitis C virus) was a matter of controversy. To determine the impact of the use of these markers on the detection of blood donors infected with hepatitis C virus, a prospective study was undertaken in Málaga (1988-1989) with 5,003 volunteer donors with two objectives: a) to know the prevalence of these non-specific markers (anti-HBc and increased serum transaminase) and antibodies to HCV (anti-C100) in our blood donor population; b) to determine whether the presence of some of these non specific markers in blood donors was associated with a higher rate of virus C infection. The prevalence of antibodies to HCV in blood donors with increased serum transaminase and/or anti-HBc was significantly higher than the prevalence found among the general blood donor population.

Biomarkers↗
PubMed1975

Immobilized glutamate oxaloacetate transaminase. Steady state kinetic analysis and stability studies.

1. Glutamate oxaloacetate transaminase (L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) was immobilized on amino ethyl cellulose using the bifunctional reagent diethyl adipimidate. 2. The steady state kinetic analysis was performed for the particulate and the free enzyme, and the Michaelis constants measured for the amino ethyl cellulose derivative were not greatly different from those measured for the free glutamate oxaloacetate transaminase, while the latter were in good agreement with values in the literature. 3. The amino ethyl cellulose-glutamate oxaloacetate transaminase was slightly more stable than the free enzyme at 65 degrees C, but was stabilised less by polyethylene glycol than the free enzyme.

Adipates↗
PubMed1988

Effect of altered hormonal states on transaminase enzymes in the genital ograns of immature female rhesus monkeys.

The effect of ovariectomy and hormone replacement therapy on the activity of glutamate oxalacetate transaminase (GOT) and glutamate pyruvate transaminase (GPT) in the oviduct, uterus, cervix and vagina of immature female rhesus monkeys (Macaca mulatta ) was studied. In intact animals, GOT activity was high in the oviduct, whereas GPT was high in the vagina. Ovariectomy suppressed the activity of both the enzymes in varying degrees. Estradiol dipropionate stimulated GOT in the oviduct and uterus, whereas progesterone increased this enzyme in the uterus. Sequential treatment of two hormones inhibited the enzymes in all the tissues; GPT was, however, stimulated in the fundus region of the uterus. The study demonstrated the presence of transaminase enzymes in the genital tissues of rhesus monkey and their differential response to sex steroids.

Journal Article↗