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Results for “ASPARTATE AMINOTRANSFERASE”

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PubMed1993

Synthesis of 3-arsonoalanine and its action on aspartate aminotransferase and aspartate ammonia-lyase. Comparison with arsenical analogues of malate and fumarate.

DL-3-Arsonoalanine has been synthesized by the Strecker synthesis from the unstable compound arsonoacetaldehyde. It inactivates pig heart cytosolic aspartate aminotransferase and inhibits aspartate ammonia-lyase by competing with aspartate (Ki/Km 0.23). The fumarate analogue (E)-3-arsonoacrylic acid and the malate analogue (RS)-3-arsonolactate also inhibit fumarate hydratase, competing with fumarate (Ki/Km 1.8) and malate (Ki/Km 1.6) respectively. Attempted non-enzymic transamination of 3-arsonoalanine gave elimination of arsenite, in contrast with the transamination of 3-phosphonoalanine, which is either successful or leads to loss of phosphate.

Alanine↗

PubMed2001

Influence of convulsants on rat brain activities of alanine aminotransferase and aspartate aminotransferase.

There exist differences between 12-day-old and adult rats in the onset of seizures induced by some inhibitors of glutamate decarboxylase (GAD). The aim of study was to investigate if there are differences between both groups in activities of rat brain alanine aminotransferase (ALT) and aspartate aminotransferase (AST), the enzymes involved in glutamate metabolism, after the administration of 3-mercaptopropionic acid as specific GAD inhibitor or isoniazid as less specific general inhibitor of pyridoxal enzymes. Activities of both aminotransferases in a supernatant 20,000 g of the whole brain (containing predominantly cytosolic isoforms of enzymes) were increased at the beginning of 3-mercaptopropionic acid-induced generalized tonic-clonic seizures. At isoniazid-induced generalized tonic-clonic seizures, a significant increase in both enzyme activities was observed in adult rat brain. In the 12-day-old rat brain, ALT and AST activities reached about 40% and about 50-60% of adult control levels, respectively. In in vitro experiments, no influence of 3-mercaptopropionic acid on transaminase activities was found and an inhibitory effect of isoniazid on the enzymes was confirmed. Increased aminotransferase activities might participate in the enhanced synthesis of excitatory amino acid neurotransmitters in the nervous system, which may take a part in the initiation of epileptic seizures. Alternatively, the increased AST activity may be connected with an increased transport of NADH from the cytosol to mitochondria, while the increased ALT activity would represent the transformation of pyruvate to alanine as a consequence of increased glycolysis.

3-Mercaptopropionic Acid↗

PubMed1982

[In vitro supplementation of pyridoxal phosphate for the optimisation of the determination of the catalytic activity of alanine aminotransferase and aspartate aminotransferase in kidney transplant patients (author's transl)].

Pyridoxal phosphate (PLP) is the coenzyme of alanine aminotransferase (ALT) and aspartate aminotransferase (AST). Thus, in vitro supplementation with PLP is important for the optimisation of the determination of catalytic activity of both enzymes. It patients with kidney transplants, stimulation by PLP is very important for ALT activity, which could be affected by plasma PLP deficiency. Furthermore, in this population catalytic activities are more frequently found increased using methods with PLP supplementation than without PLP supplementation (56% and 71% of patients for AST and ALT, respectively). These differences are not related to HBs antigen.

Adolescent↗

PubMed2002

[Twin test in the determination of alanine aminotransferase and aspartate aminotransferase in the serum].

OBJECTIVE: To explore a method which can simultaneously determine alanine aminotransferase (ALT) and aspartate aminotransferase (AST) in the serum. METHODS: Using the self-prepared twin test reagent, ALT and AST in the serum were detected simultaneously. RESULTS: There was a good correlation between the twin test's method and the traditional method in the detection of ALT and AST (All r = 0.999). The precision of the method was good, and the coefficient variation (CV) was below 5%. Hemolysis, jaundice, and lipohemia serum were found to be interference-free. The time of the detection was two times of the traditional method. CONCLUSION: The twin test method can both exert the capability of the automatic analyzer and shorten the time of detection. It is a method worthy to be popularized.

Alanine Transaminase↗

PubMed2006

Effect of acarbose on alanine aminotransferase and aspartate aminotransferase activities in the liver of control and diabetic CBA mice.

The purpose of this study was to examine the short-term effects of diet containing 0.1% (m/m) of acarbose in standard laboratory chow on specific liver enzyme activities: alanine aminotransferase (ALT) and aspartate aminotransferase (AST) in control and diabetic CBA mice. Diabetes was induced by intravenous injection of alloxan monohydrate in a dose of 75 mg kg(-1) mouse body mass seven days before the treatment with acarbose. There were four groups of CBA mice in the experiment: control (C) mice (n = 6) and diabetic (D) mice (n = 8) fed standard chow; control (C/A-100) mice (n = 8) and diabetic (D/A-100) mice (n = 8) fed standard chow containing 0.1% acarbose. Diabetes induced a decrease of the ALT catalytic activities to 69.6% of the control value. A similar level of decreased ALT catalytic activity was detected in the liver of control and diabetic mice fed chow containing 0.1% acarbose. No changes in the specific and total activities of AST in the liver of experimental groups were observed.

Acarbose↗

PubMed1996

In vitro effects of the novel anti-epileptic agent vigabatrin on alanine aminotransferase and aspartate aminotransferase activities in rat serum.

The in vitro effects of vigabatrin (CAS 60643-86-9, MDL 71,754) on alanine aminotransferase (ALT) and aspartate aminotransferase (AST) activities were examined in rat serum. Initially, vigabatrin (30-100 micrograms/ml) produced a concentration-dependent decrease in ALT activity at 100 micrograms/ml or more after 15 min incubation with the rat serum. AST activity, in contrast, was unaffected by concentrations up to 1,000 micrograms/ml. Next, treating the rat serum with vigabatrin (30-300 micrograms/ml) for up to 5 h produced a concentration- and time-dependent decrease in ALT activity. On the other hand, a decrease in AST activity was observed only after incubation with the highest concentration of vigabatrin for 3 h or more. Finally, an investigation was made on the antagonistic effect of L-alanine, a natural substrate for ALT, on the vigabatrin-induced decrease in ALT activity to elucidate possible mechanisms underlying the inhibitory effect of vigabatrin on ALT activity. L-alanine, depending on its concentration, countered the effects of vigabatrin (100 micrograms/ml) at a 10- or 100-fold higher molar ratio than vigabatrin. These findings suggest that vigabatrin favorably decreases ALT activity by blocking the L-alanine binding site of enzymes.

Alanine↗

PubMed1995

Effects of mebendazole, albendazole and praziquantel on alanine aminotransferase and aspartate aminotransferase of Echinococcus granulosus cyst wall harbored in mice.

Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) of Echinococcus granulosus cyst wall harbored in mice for 10-12 months was measured. The activities of the 2 enzymes were 3,430 +/- 1,370-4,160 +/- 1,790 and 1,560 +/- 840-2,890 +/- 1,470, respectively. When infected mice were treated ig with mebendazole (Meb) 25 mg.kg-1.d-1 for 7-14 d, or 50 mg.kg-1.d-1 for 7 d, the ALT activities of cyst walls of both collapsed and full cysts were inhibited significantly with average inhibition rates of about 50%. Another benzimidazole derivative, albendazole (Alb), also inhibited ALT activity of the cyst wall with an inhibition rate of 40.7%, but this was not the case in the treatment with praziquantel 500 mg.kg-1.d-1 of the infected mice for 14 d. When the infected mice were treated ig with the above mentioned drugs at the same regimens, no apparent effect on AST activities of the cyst wall was seen except for the group treated ig with Meb at a higher daily dose, the inhibition rates being 26% (collapsed cyst) and 43.9% (full cyst). The significance of the results has been discussed briefly.

Alanine Transaminase↗

PubMed1996

Activities of glycogen phosphorylase, alanine aminotransferase and aspartate aminotransferase in adult worms of Litomosoides carinii recovered from pyridoxine deficient cotton rats (Sigmodon hispidus).

This paper demonstrates that the activities of glycogen phosphorylase (GP), alanine aminotransferase (ALT) and aspartate aminotransferase (AST) are reduced in adult worms of the filarial nematode Litomosoides carinii recovered from pyridoxine-deficient cotton rats when compared to worms recovered from pyridoxine-sufficient controls. GP, ALT and AST activities were determined in adult worms L. carinii recovered from cotton rat hosts over a 20-week experimental period. Activities of GP, ALT and AST in the parasite showed a direct correlation with the dietary pyridoxine intake of their host. Throughout the experiment, enzyme activities were significantly lower (P < 0.001) in worms from rats fed a pyridoxine-free diet ad libitum that in worms from rats fed either a stock colony diet, a pyridoxine-free diet ad libitum with daily supplementation of 100 micrograms pyridoxine or limited amounts of pyridoxine-free diet with daily supplementation of 100 micrograms pyridoxine. The lower than normal activity of GP, ALT, AST and other enzymes dependent on the biologically active derivative of pyridoxine, the coenzyme pyridoxal-5-phosphate (PLP), interferes with the protein, carbohydrate and lipid metabolism of L. carinii and may in part cause the reduced establishment, development and growth of the parasite in pyridoxine-deficient hosts.

Alanine Transaminase↗

PubMed1986

Serum alanine aminotransferase to aspartate aminotransferase ratio and degree of fatty liver in morbidly obese patients.

We evaluated the change in serum alanine aminotransferase (ALT; EC 2.6.1.2) to serum aspartate aminotransferase (AST; EC 2.6.1.; ALT/AST) ratio with the degree of fatty liver in morbidly obese patients. A total of 31 patients were included in the study. Fatty liver was graded as 0 to 4+. The mean and SD of AST and ALT were not significantly different between groups of patients with various grades of fatty liver. There was, however, a significant correlation between the ALT/AST ratio and the degree of fatty infiltration of the liver. This, we believe, implies damage mainly to the plasma membrane allowing loss of cytoplasmic enzymes rather than loss of mitochondrial enzymes.

Adult↗

PubMed2004

[Prevalence of hepatitis A, B, C and E virus markers among patients with elevated levels of Alanine aminotransferase and Aspartate aminotransferase in Phnom Penh (Cambodia) and Nha Trang (Central Vietnam)].

In order to describe the respective part of viral hepatitis in liver diseases observed in Cambodia and Vietnam, ninety consecutive patients with Aspartate aminotransferase (AST) and Alanine aminotransferase (ALT) > or = 100 Ul/l were tested for hepatitis A, B, C and E markers in Phnom Penh and Nha Trang. The markers were IgM antibodies to hepatitis A virus (anti-HAV IgM), hepatitis B surface antigen (HBsAg), antibodies to hepatitis C virus (anti-HCVAb) and IgG antibodies to hepatitis E virus (anti-HEV IgG). Recruited patients were predominantly adults and male (sex ratio 76%). Among these patients, 81% were tested positive to at least one marker in Nha Trang and 79% in Phnom Penh. In Nha Trang, HBsAg was more frequent (73%) than anti-HCV Ab (9%) while in Phnom Penh both markers were closely similar (HBsAg: 41%, anti-HCV Ab: 39%). In both population samples, HBsAg was more prevalent among young people whereas anti-HCV Ab were only detected in adults. No case of acute HAV infection was diagnosed in Nha Trang while anti-HAV IgM were detected in 20% of Cambodian patients. Anti-HEV IgG were infrequent (2% in Nha Trang, 5.5% in Phnom Penh). Only one case was notified, a male Vietnamese patient probably suffering from acute hepatitis E. More studies would be useful to improve the control measures against viral hepatitis in the public health programs.

Adolescent↗

PubMedDate not supplied

Observations of alanine aminotransferase and aspartate aminotransferase in THRIVE studies treated orally with ximelagatran.

Treatment of acute venous thromboembolism (VTE) and prophylaxis of recurrent events has been investigated in the THRIVE (THRombin Inhibitor in Venous Thrombe Embolism) Treatment and the THRIVE III trial using the oral direct thrombin inhibitor ximelagatran. Alanine aminotransferase (ALAT) increased in 9.6% and 6.4% of patients in the THRIVE Treatment and THRIVE III trials, respectively. The authors analysed the time course of the ALAT and in additionally of aspartate aminotransferase (ASAT) in blood from 52 and 23 patients participating in the THRIVE Treatment and the THRIVE III trials in Germany. Analysis of variance for repeated measures and t test were performed. In the THRIVE Treatment trial, ALAT was significantly higher at week 2 for enoxaparin/warfarin (p => .0039, t test) and at months 3 and 6 for ximelagatran (p = .0453, p = .0014, respectively). ASAT and ASAT/ALAT ratio values did not increase and not differ for both groups. In the THRIVE III trial, ALAT and ASAT did not increase and did not differ compared to the comparator placebo. 2 x 36 mg Ximelagatran, induced higher ALAT values at months 3 and 6 compared to 2 x 24 mg ximelagatran (p = .0105, p = .0063, respectively). ASAT did not differ between the two doses of ximelagatran. The ASAT/ALAT ratios were lower at week 2 for enoxaparin/warfarin (t-test, p = .0032) and at month 3 and 6 for 2 x 36 mg versus warfarin or 2 x 24 mg Ximelagatran (p between .0187 and .0002). The authors conclude that ALAT increases dose dependently during therapy with ximelagatran. The less frequent and lower increase of ASAT values compared to ALAT values indicates a nontoxic effect of ximelagatran on liver cells.

Administration, Oral↗

PubMed1984

Organ specificity of glucocorticoid-sensitive tyrosine aminotransferase. Separation from aspartate aminotransferase isoenzymes.

In order to study whether hormone-sensitive tyrosine aminotransferase exists in tissues other than liver, we have devised means to separate the liver-specific enzyme from other enzymes that transaminate tyrosine and to distinguish between the authentic enzyme and the principal "pseudotyrosine aminotransferases," which are the isoenzymes of aspartate aminotransferase. We accomplish this by suppressing proteolysis of the authentic enzyme using a buffer of pH 8.0 containing 0.1 M potassium chloride; enzyme extracted from liver in this buffer migrates as a single peak during chromatography on hydroxylapatite and represents the undegraded native form. A much smaller peak of tyrosine aminotransferase activity elutes at higher ionic strength and corresponds to a mixture of mitochondrial aspartate aminotransferase and partially degraded tyrosine aminotransferase. Cytosolic aspartate aminotransferase, in contrast, adsorbs weakly to the hydroxylapatite column and transaminates tyrosine very poorly although it readily utilizes monoiodotyrosine. The aspartate aminotransferase isoenzymes separate completely from tyrosine aminotransferase during chromatography on DEAE-Sepharose CL-6B. By combining these techniques with the use of specific antibodies, we show that brain, heart, and kidney do not contain tyrosine aminotransferase. Furthermore, we locate both isoenzymes of aspartate aminotransferase on polyacrylamide gels and show that both react histochemically as tyrosine aminotransferases when monoiodotyrosine is used as substrate. Use of these techniques, therefore, permits unambiguous identification of tyrosine aminotransferase and its separation from the background of nonspecific transamination.

Animals↗

PubMedDate not supplied