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PubMed1985

Marked elevation of serum transaminase activity associated with extrahepatic biliary tract disease.

Nine patients with choledocholithiasis or cholelithiasis developed transient elevations of serum glutamic oxalacetic transaminase (SGOT) levels of greater than 600 units. Awareness of such transient biliary disease will prevent an unnecessary evaluation of a primary hepatocellular disorder. In our study, we concluded that 1) The SGOT level rose and fell rapidly within a 24- to 72-hour period. 2) Higher SGOT levels were seen in patients with choledocholithiasis in whom the gallbladder had been removed. 3) In patients with choledocholithiasis a fall in SGOT level did not necessarily mean the stone had passed.

Adult↗

PubMed1991

Glutamate Oxaloacetate Transaminase in Pea Root Nodules : Participation in a Malate/Aspartate Shuttle between Plant and Bacteroid.

Glutamate oxaloacetate transaminase (l-glutamate: oxaloacetate aminotransferase, EC 2.6.1.1 [GOT]), a key enzyme in the flow of carbon between the organic acid and amino acid pools in pea (Pisum sativum L.) root nodules, was studied. By ion exchange chromatography, the presence of two forms of GOT in the cytoplasm of pea root nodule cells was established. The major root nodule form was present in only a small quantity in the cytoplasm of root cells. Fractionation of root nodule cell extracts demonstrated that the increase in the GOT activity during nodule development was due to the increase of the activity in the cytoplasm of the plant cells, and not to an increase in activity in the plastids or in the mitochondria. The kinetic properties of the different cytoplasmic forms of GOT were studied. Some of the K(m) values differed, but calculations indicated that not the kinetic properties but a high concentration of the major root nodule form caused the observed increase in GOT activity in the pea root nodules. It was found that the reactions of the malate/aspartate shuttle are catalyzed by intact bacteroids, and that these reactions can support nitrogen fixation. It is proposed that the main function of the nodule-stimulated cytoplasmic form of GOT is participation in this shuttle.

Journal Article↗

PubMed1975

31P nuclear-magnetic-resonance studies of pyridoxal and pyridoxamine phosphates. Interaction with cytoplasmic aspartate transaminase.

The 31P nuclear magnetic resonance (NMR) spectrum of the phosphate in free pyridoxal or pyridoxamine phosphate reveals a resonance signal that is coupled to the methylene protons of the 5-CH2 with JHP of 6.0 +/- 0.3 Hz. Proton noise decoupling results in a single signal with a pH-dependent chemical shift with deprotonation of the phosphate resulting in a shift of the 31P resonance to lower fields. A single 31P NMR signal at a frequency corresponding to fully ionized phosphate monoesters is observed in aspartate-transaminase-bound pyridoxal or pyridoxamine phosphate. The 31P resonance in the holotransaminase is pH-independent and is unaffected by saturating concentrations of substrates or inhibitors. Only denaturation with 6 M guanidine with HCl results in changes in the 31P of the holoenzyme. It appears that the phosphate group of pyridoxal phosphate is bound to a positive pocket in the holoenzyme and remains fully ionized in the pH range of 5.6 to 9.2. The phosphate-binding properties are present even in the apoenzyme which is able to bind inorganic phosphate which then can be displaced by pyridoxal or pyridoxamine phosphate in the process of holoenzyme formation.

Animals↗

PubMed1982

Mapping studies on human mitochondrial glutamate oxaloacetate transaminase.

Data from six primary hybrids and twenty-two subclones have confirmed the assignment of the mitochondrial form of glutamate oxaloacetate transaminase to chromosome 16. Family studies have provided independent confirmation of this and have suggested the gene order PGP-16qh-GOT2-HP. These studies were made easier by the development of a new stain for the detection of GOT activity.

Animals↗

PubMed1970

Genetic polymorphisms of human mitochondrial glutamic oxaloacetic transaminase.

In a survey of 860 unselected human placental extracts, three variants of mitochondrial glutamic oxaloacetic transaminase were found, all of which were common enough to be considered polymorphisms. Family studies showed that this enzyme is under the control of nuclear rather than mitochondrial DNA.

Aspartate Aminotransferases↗

PubMed1970

Australia antigen in a closed adult population monitored for serum glutamic oxalacetic transaminase.

A study of the presence of Australia antigen (Au/SH) was conducted over a period of 21 weeks among volunteer plasma donors living in a prison and being monitored for serum glutamic oxalacetic transaminase (SGOT). A good correlation was observed between the level of SGOT and presence of Au/SH, the latter being present in 33% of donors with SGOT values higher than 101 Karmen units and in 12% of those with SGOT values of 41 to 100 units. Furthermore, none of the 87 donors with all SGOT values below 40 was found positive for Au/SH. It should be noted, however, that single specimens only were tested from 72 of the 87 individuals. Au/SH was detected with equivalent efficiency by both agar gel precipitation and complement fixation procedures. Implications of these findings in the prognostication of hepatitis carrier state are discussed.

Adolescent↗

PubMed1970

Enhancement of glutamic-pyruvic transaminase activity in leptospirae by addition of rabbit serum.

Glutamic-pyruvic transaminase (GPT) in leptospirae was shown to have an optimal temperature of 30 C and pH 8.0. It was activated by cofactor pyridoxal phosphate, similar to GPT from other sources. However, GPT in all leptospirae, such as Leptospira canicola, L. icterohaemorrhagiae, L. autumnalis, and L. biflexa, evidently had less activity even when pyridoxal phosphate was present, in comparison with the cultivable spirochete Reiter treponeme and Streptococcus faecalis. The low level of activity of leptospiral GPT was enhanced more than 2.5-fold by the addition of about 10% rabbit serum, whereas GPT of S. faecalis did not show such enhancement. Enhancement of leptospiral GPT was greater with rabbit serum than with bovine or horse serum.

Journal Article↗

PubMed1976

Lactate dehydrogenase and aspartete transaminase of the cerebrospinal fluid in patients with brain tumours, congenital hydrocephalus, and brain abscess.

The diagnostic value of CSF lactate dehydrogenase and aspartate transaminase in cases of brain tumours (except for CSF AST in the benign tumours), congenital hydrocephalus, and brain abscess is established. Tumour cyst fluids show a higher enzymatic activity than does the CSF. The two enzyme estimations do not help in differentiating the supratentorial from the infratentorial tumours. CSF AST is superior to CSF LD in discriminating the malignant and benign tumours, in so far as the AST is increases selectively in malignancy. Estimates of CSF LD are slightly superior to those of CSF AST, both in incidence of abnormality and the degree of their rise.

Aspartate Aminotransferases↗

PubMed1983

Serum uric acid, inorganic phosphorus, and glutamic-oxalacetic transaminase and blood pressure in carbohydrate-sensitive adults consuming three different levels of sucrose.

12 men and 12 women, classified as carbohydrate-sensitive on the basis of an exaggerated insulin response to a sucrose load, consumed diets containing either 5, 18, or 33% sucrose in a crossover design. The diets simulated the average American diet and consisted of identical natural and processed foods with the exception of a patty. The patty provided the experimental levels of sucrose; the difference was made up by starch. Each level of sucrose was consumed for a 6-week period. Subject body weights were maintained. Fasting serum uric acid and inorganic phosphorus increased as the level of dietary sucrose increased. Diastolic blood pressure was significantly higher when subjects were on the 33% sucrose diet as compared to the 5 and 18% diets. Serum glutamic-oxalacetic transaminase was not affected by diet. In tolerance tests after a sucrose load (2 g/kg body weight), the uric acid response was higher after the 18 and 33% sucrose diets than after the 5% sucrose diet. Serum inorganic phosphorus, which increased significantly with each level of dietary sucrose, decreased following the sucrose load. These results indicate that carbohydrate-sensitive individuals may be affected adversely by the level of sucrose commonly found in the Westernized diet. Since elevated serum uric acid and blood pressure have been identified as risk factors in degenerative diseases, this study suggests that carbohydrate-sensitive individuals should limit their sucrose consumption.

Adult↗

PubMed1985

Sialic acid content of erythrocytes in uremic patients. Correlation with the age distribution of erythrocytes as assessed by glutamic oxaloacetic transaminase determination.

In a previous study we suggested that an enrichment in young red blood cells (RBC) should occur in the erythrocyte population of uremic-anemic patients. This change in RBC age distribution together with the fact that young cells were reported to be richer in sialic acid would provide an explanation for the observed lack of difference in sialic acid content between patients' and controls' whole erythrocyte populations in spite of an increased neuraminidase activity found to be present in patients' serum. To verify this assumption glutamic oxaloacetic transaminase (GOT) activity, which is an erythrocyte age index, and sialic acid were determined in low and high density fractions separated by centrifugation of packed cells representing young and old RBC, respectively, from two groups of 8 individuals with chronic renal failure and two groups of controls. GOT was determined also in whole erythrocyte populations. Mean GOT activity was significantly higher in the young fractions compared to the old of both patients' and control RBC (14.9 vs. 7.8 and 12.4 vs. 7.5 IU/g Hb). Activity of the whole RBC population was significantly higher in uremics as compared to controls (11.7 vs. 5.6 IU/g Hb) which is compatible with a lower median erythrocyte age. Mean sialic acid was higher in the young fractions as compared to the old (42.7 vs. 35.3 nmol/10(9) cells in controls and 48.9 vs. 43.0 nmol/10(9) cells in patients). These differences together with an enrichment in young cells would compensate for the eventual loss of sialic acid in the whole population resulting from an increased neuraminidase-like activity in patients' serum.

Aspartate Aminotransferases↗

PubMed1976

Serum iron, glutamic oxalacetic transaminase and creatine phosphokinase in acute myocardial infarction. A comparative study.

The serum iron was subnormal on the first three days, following acute myocardial infarction in thirty patients. This is significantly less than the incidence of abnormalities demonstrated by assays of creatine phosphokinase (CPK) and glutamic oxalacetic transaminase (SGOT) in serum. Occasional patients had abnormal serum iron concentrations in association with normal CPK activities. For this reason serum iron determination may usefully supplement CPK activity measurements and possibly those of SGOT activity as an aid to the detection of acute myocardial infarction.

Adult↗

PubMed1986

A direct assay for pyridoxal 5'-phosphate using pig heart apo-aspartate transaminase.

The development of a simple enzymatic method for the determination of blood and plasma pyridoxal 5'-phosphate (PLP) using pig heart apo-aspartate transaminase (apo-AST) is described. The technique requires three steps: sample extraction using perchloric acid, a binding step in which PLP in the sample extract is attached to the apo-AST and the enzymatic assay of the reconstituted holo-AST. PLP extracts were analysed with and without a known concentration of added PLP to correct for variation in recovery between different specimens. Procedures are outlined for manual and automatic analysis of the PLP extracts. Using the KONE Clinical Analyser after the extraction step, it is possible to measure enzyme activity in 100 specimens (i.e. 400 tubes) in a 5 h period. Results are shown from 185 healthy women aged 20-45 years, in which plasma PLP concentrations ranged from 5 to 165 nmol/L, and 142 men and 56 women in government service aged 17-64 years, whose plasma PLP ranged from 8 to 169 nmol/L. Values less than 20 nmol/L are believed to indicate vitamin B6 deficiency and the method is able to measure 5 nmol/L.

Adolescent↗

PubMedDate not supplied

Effect of the dietary fatty acid component on the release of 14C-taurocholate, 14C-bilirubin, alkaline phosphatase, and aspartate transaminase by isolated rat liver cells.

Rats were fed liquid diets for 7 days containing either triolein or Liposyn, which is rich in linoleic acid, as fat sources, and liver cell suspensions were prepared following collagenase perfusion. The release from isolated cells of alkaline phosphatase and aspartate transaminase during a 3-hr incubation did not differ. The uptake and release of 14C-taurocholate during a brief incubation was lower but not significantly in Liposyn-fed rats (0.1 greater than p greater than 0.05): the uptake was 9.74 +/- 1.58 vs 16.7 +/- 3.3 nmol/mg protein in triolein-fed rats; the release was 3.17 +/- 0.65 vs 5.35 +/- 1.01 nmol/mg protein in triolein-fed rats. The uptake of 14C-aminolevulinic acid was similar in both groups, but release of 14C-bilirubin during a 30-min incubation was 5,420 +/- 1010 in the Liposyn group vs 12,030 +/- 2,200 dpm/mg protein in the triolein group (p = 0.02). It is concluded that a diet high in linoleic acid decreases bilirubin release in isolated liver cells consistent with the ability of this diet to cause cholestasis in vivo.

Alkaline Phosphatase↗

PubMed1981

Glutamic-oxalacetic transaminase leakage from human spermatozoa as an indicator of cryodamage.

The levels of extracellular glutamic-oxalacetic transaminase (GOT: EC 2.6.1.1) activity have been measured in cell-free supernatants of human semen and of semen + cryoprotectant mixtures both before freezing by either cryostorage or quench-freezing regimes, and after subsequent thawing. The mean level of GOT activity in seminal plasma was 293 (+/- 15 sem) IU/l at 37 degrees C, this being 15 times the level in normal blood plasma. Seminal GOT is positively correlated (p less than 0.001) with the sperm density. Increases in the extracellular GOT activity were measured after both cryostorage and quench-freezing, but the latter procedure, which destroys all sperm motility, caused an average of 2.8 times more enzyme release than cryostorage. Although the release of GOT from human spermatozoa during freezing and thawing does not correlate with the commonly used percent return of motility as an estimate of cryosurvival, possible explantations for this finding, and its importance, are discussed. Objective measurements such as GOT release may be developed to augment, if not replace, subjective estimations of sperm motility as indicators of cellular integrity in studies of sperm cryostorage.

Aspartate Aminotransferases↗

PubMed1976

Improved and effective assays of the glutamic oxaloacetic transaminase by the coenzyme-apoenzyme system (CAS) principle.

Standardized and reliable methods have been devised to assay preparations of the glutamic oxaloacetic transaminase from human erythrocytes by the CAS principle, i.e., the unsaturation and saturation of the coenzyme (pyridoxal 5'-phosphate) of a Coenzyme-Apoenzyme System. This dual enzymic assay is effective to detect and measure human deficiencies of vitamin B6. A preferred procedure has been developed, particularly for individuals and for limited groups, but is also applicable to large groups. A simplified procedure, which emphasizes the statistical significance of difference between large groups was also developed. Lyophilized erythrocyte hemolysates appear stable for up to 7 days for simplified transportation.

Apoenzymes↗

PubMed1978

The effect of glycerol and dilution on the release of glutamic oxaloacetic transaminase from chicken spermatozoa.

Glycerol was added to washed chicken spermatozoa to determine its effect on the release of glutamic oxaloacetic transaminase (GOT). The addition of up to 2.191 M glycerol did not cause a release of GOT when it was added as part of the diluent. GOT was released, however, following rapid decreases in the glycerol concentration of a diluent. The amount of GOT released was related to the rate of change in molarity of glycerol.

Animals↗

PubMed1985

Glutamic oxaloacetic transaminase released from chicken spermatozoa during freeze-thaw procedures.

The feasibility of using glutamic oxaloacetic transaminase (GOT) released from chicken spermatozoa for evaluation of freeze-thaw damage and the optimum concentration of glycerol on the basis of GOT release were examined. There was a highly significant correlation (-.88) between sperm motility in media containing various concentrations of glycerol and GOT activity in extracellular media after freeze-thawing. This indicates that GOT activity in the supernatant of frozen-thawed semen may be useful as an indicator for frozen-thawed injury of chicken spermatozoa. The amounts of GOT released from spermatozoa after 20 min of glycerol equilibration at 5 C gradually increased from 1 to 18% glycerol. The GOT activity in the extracellular medium after freeze-thawing was lowest at 10% glycerol. To estimate GOT leakage from spermatozoa during the freeze process, except glycerol equilibration, the amounts of GOT just before freezing were subtracted from the amounts of GOT after freeze-thawing. The minimum difference between GOT leakage before and after freeze-thawing was shown to be at 16% glycerol.

Animals↗

PubMed1976

Observations on decreased serum glutamic oxalacetic transaminase (SGOT) activity in azotemic patients.

Serum glutamic oxalacetic transaminase (SGOT) activity may be decreased or even absent in patients with uremia. We correlated urea concentration with SGOT activity by the automated Rush (AutoAnalyzer, Techicon Instruments Corp., Tarrytown, New York) method (SGOT, SMA) and by the Henry-Karmen kinetic assay (SGOT, K). Extremely low SGOT (SMA) activity (less than 10 IU) was found in 6% of 5030 consecutive samples, and 71% of them occurred in patients with azotemia. SGOT activity was inversely proportional to urea concentration. A similar but less obvious pattern was observed with the SGOT (K) assay. SGOT activity increased significantly after hemodialysis in a group of 16 patients studied by both methods. It was not inhibited either by urea or uremic serum added in vitro. The explanation for this phenomenon is not known.

Adult↗