• Parasites, Hosts and Diseases
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• v.21 no.1
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• pp.41-48
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• 1983

The activity and distribution of aspartate aminotransferase (EC 2.6. 1. 1) and alanine aminotransferase (EC 2.6.1.2) in adult Fascicle hepatica have been studied. Fasciola hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of GOT and GPT was measured by the method of Reitman and Frankel. Isozyme patterns of those enzyme were also examined by DEAE-cellulose column chromatography. The results obtained were as follows; 1. The activity of aspartate and alanine aminotransferase was about 0.55 unit and 0.92 unit per 1g of Fascicle hepatica, respectively. 2. The activity of those enzymes was relatively low compared with those in mammalian tissues. 3. The distribution of aspartate aminotransferase in the subcellular organelles showed that 71% of the activity was in cytosolic, 24% in mitochondrial and 5% was in nuclear fraction. 4. About 22% of the total alanine aminotransferase activity was found in the mitochondrial fratstion, about 66% in the cytosolic fraction. 5. Aspartate aminotransferase from cytosolic fraction was separated into two types of isozymes, whereas alanine aminotransferase from cytosolic fraction gave only one active peak on DEAE-cellulose column chromatography.

• Korean Journal of Microbiology
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• v.31 no.3
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• pp.237-244
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• 1993

Aspartate aminotransferase (ASAT) (L-aspartate : 2-oxyoglutarate, EC 2.6. 1. 1.) from Streptomyces fradiae NRRL 2702 has been purified by acetone precipitation, DEAE-cellulose, hydroxyapatite, and preparative electrophoresis (Prep cell), of which the last was the most effective step in the purification of ASAT. The molecular mass was estimated to be 54,000 dalton by SDS-PAGE and 120,000 dalton by gel filtration chromatography. Preparative isoelectric focusing of purified ASAT resulted in one polypeptide band with a pI of 4.2, showing homogeneity and indicating that the enzyme is composed of two identical subunits. The enzyme was specific for L-aspartate as an amino donor ; the $K_{m}$ values were determined to be 2.7 mM for L-aspartate, 0.7 mM for 2-oxoglutarate, 12.8 mM for L-glutamate, and 0.15 mM for oxaloacetate. The enzyme was relatively heat-stable, having maximum activity at 55.deg.C, and it had a broad pH optimum ranging from 5.5 to 8.0. The activity of the purified enzyme was not inhibited by ammonium ions. This paper reports the first purification and characterization of the aspartate aminotransferase from a species of Streptomyces.s.

• Journal of Applied Biological Chemistry
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• v.52 no.3
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• pp.109-115
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• 2009

The gene encoding a putative aspartate aminotransferase in Xanthomonas oryzae pv. oryzae (Xoo) was cloned using PCR technique. The gene was ligated with pET-21(a) vector containing His6 tag and expressed in E. coli BL21(DE3). Affinity purification of the recombinant aspartate aminotransferase with Ni-NTA resin resulted in one band by SDS-PAGE analysis. The purified enzyme showed a molecular weight of 43 kDa, as expected. The enzyme was the most active toward L-aspartate as an amino donor, indicating that the purified enzyme is one of aspartate aminotrans-ferases exist in Xoo. Optimal activity of the enzyme was observed at around pH 7.5 and stability was much higher at alkaline pH rather than acidic pH values. The enzyme was considerably activated by the presence of manganese ion, showing about 157% of control activity at 1.0 mM.

• Asian-Australasian Journal of Animal Sciences
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• v.27 no.12
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• pp.1744-1748
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• 2014

A dose-response experiment with seven supplemental pyridoxine levels (0, 0.66, 1.32, 1.98, 2.64, 3.30, and 3.96 mg/kg) was conducted to investigate the effects of pyridoxine on growth performance and plasma aminotransferases and homocysteine of White Pekin ducks and to estimate pyridoxine requirement for these birds. A total of 336 one-day-old male White Pekin ducks were divided to 7 experimental treatments and each treatment contained 8 replicate pens with 6 birds per pen. Ducks were reared in raised wire-floor pens from hatch to 28 d of age. At 28 d of age, the weight gain, feed intake, feed/gain, and the aspartate aminotransferase, alanine aminotransferase, and homocysteine in plasma of ducks from each pen were all measured. In our study, the pyridoxine deficiency of ducks was characterized by growth depression, decreasing plasma aspartate aminotransferase activity and increasing plasma homocysteine. The ducks fed vitamin $B_6$-deficient basal diets had the worst weight gain and feed/gain among all birds and this growth depression was alleviated (p<0.05) when pyridoxine was supplemented to basal diets. On the other hand, plasma aspartate aminotransferase and homocysteine may be the sensitive indicators for vitamin $B_6$ status of ducks. The ducks fed basal diets had much lower aspartate aminotransferase activity and higher homocysteine level in plasma compared with other birds fed pyridoxine-supplemented diets (p<0.05). According to quadratic regression, the supplemental pyridoxine requirements of Pekin ducks from hatch to 28 days of age was 2.44 mg/kg for feed/gain and 2.08 mg/kg for plasma aspartate aminotransferase and the corresponding total requirements of this vitamin for these two criteria were 4.37 and 4.01 mg/kg when the pyridoxine concentration of basal diets was included, respectively. All data suggested that pyridoxine deficiency could cause growth retardation in ducks and the deficiency of this vitamin could be indicated by decreasing plasma aspartate aminotransferase activity and increasing plasma homocysteine.

• Journal of Nutrition and Health
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• v.19 no.4
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• pp.246-254
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• 1986

Weanling female Sprague Dawley rats were fed d diets containing 22mg pyridoxine. BCI/kg diet (control diet) and l.2mg pyridoxine. BCI/kg diet (deficient diet). One control group and one defi­c dent group were fed their diet throughout growth, g gestation and lactation. After the pups were born and weaned, the deficient group was divided into two groups. One switched to control diet(supple­I mented group) and the other continued the same d deficient diet( deficient group) until 10 week -old. The liver mitochondrial and cytosolic asparate a aminotransferase activity and pyridoxal phosphate content were determined in offspring rats. The aspartate aminotransferase activities in both liver mito$\phi$ondrial and cytosolic fractions of den­d cient group were significantly lower than those of controls, but there were no significant differences between two groups after addition of 1O^{-4}M pyri­d do뼈I phosphate to the medium. By pyridoxine s supplementation after weaning, the reduced aspar­a tate aminotnmsferase activities were only partialy I restored to control levels. The pyridoxal phospha­t te content of deficient group in Iiver mitochondr­ial and cytosoIic fractions were alo significantly different from those of controls, but readily restored by dietary supplementation. These results suggest that there is a quantitative and a qualitative changes of aspartate amino trans­f ferase and pyridoxal phosphate in liver mitochon­d drial and cytosolic fraction by long-term pyrido­x xine deficiency and these reductions can partially recovered by dietary pyridoxine supplementation after weaning.

• International Journal of Industrial Entomology and Biomaterials
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• v.15 no.1
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• pp.59-68
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• 2007

Changes in protein metabolism were studied in hemolymph and fat body on days 1, 3, 5 and 7 of the fifth-instar silkworm, Bombyx mori, exposed to lethal, sublethal doses and prevailing levels of fluoride in groundwater in Karnataka and Andhra Pradesh States of India. The total protein content indicated a depletion followed by a concomitant increase in accumulation of free amino acids. Concurrently, the activity of protease in both of the tissues was also increased. A steady enhancement in the activities of alanine aminotransferase and aspartate aminotransferase paralleled the elevation of glutamate dehydrogenase activity in the tissues studied. It is presumed, on the basis of these results, that the fluoride toxicity causes major changes in protein metabolism of the silkworms.

• Biomolecules & Therapeutics
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• v.10 no.4
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• pp.211-217
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• 2002

Hepatoprotective activity of methanol extract of Angelica tenuissima Nakai on the $CCl_4$-induced hepatotoxicity was investigated. To elucidate the hepatoprotective activity and free radical scavenging effect, we examined alanine aminotransferase (ALT), aspartate aminotransferase (AST), albumin, total protein, cholesterol, malondialdehyde (MDA) levels in serum and activities of superoxide dismutase (SOD), catalase (CAT) in hepatic tissue as compared with those of carbon tetrachloride-induced rats. The action mechanism also has been estimated by quantative analysis of cytochrome P450 (CYP), NADPH-CYP reductase for phase I metabolism and glutathion (GSH), glutathion S-transferase (GST) level for phase II metabolsim. Treatment of Angelica tenuissima methanol extract significantly lowered the levels of alanine aminotransferase and aspartate aminotransferase. In addition, the levels of cholesterol, triglyceride, MDA, CAT were decreased, and SOD was activated. This result indicates that the hepatoprotective effect of Angelica tenuissima methanol extract on the CCl4-induced hepatotoxicity would be originated from reduction of the NADPH-CYP reductase, GSH and the enhancement of the activities of GST, CYP.

• Journal of Periodontal and Implant Science
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• v.22 no.2
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• pp.214.2-214.2
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• 1992

• Journal of Food Hygiene and Safety
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• v.14 no.2
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• pp.172-178
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• 1999

Previous studies have shown that methanol extract and its butanol fraction of Carthamus tinctorius L. Semen have the hepatoprotective effect on the CCl4-induced hepatotoxicity. The hepatoprotective effect of subfractions has been evaluated by analyzing blood and hepatocyte biochemical analyses and biotransformation enzyme analyses. Treatment of BS-5, subfraction has significantly decreased the activities of alanine aminotransferase and aspartate aminotransferase. In addition, the levels of cholesterol and triglyceride in liver have been decreased as compared with that of CCl4 treated rats. The hepatoprotective effect of BS-5, subfraction on the CCl4-induced hepatotoxicity would be mediated of the attenuation of the level of cytochrome P450 and the enhancement of the activity of glutathion S-transferase.

• The korean journal of orthodontics
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• v.45 no.5
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• pp.261-267
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• 2015

Objective: To measure aspartate aminotransferase (AST) activity in the pulp of teeth treated with fixed appliances for 6 months, and compare it with AST activity measured in untreated teeth. Methods: The study sample consisted of 16 healthy subjects (mean age $25.7{\pm}4.3$ years) who required the extraction of maxillary premolars for orthodontic reasons. Of these, 6 individuals had a total of 11 sound teeth extracted without any orthodontic treatment (the control group), and 10 individuals had a total of 20 sound teeth extracted after 6 months of orthodontic alignment (the experimental group). Dental pulp samples were extracted from all control and experimental teeth, and the AST activity exhibited by these samples was determined spectrophotometrically at $20^{\circ}C$. Results: Mean AST values were $25.29{\times}10^{-5}U/mg$ (standard deviation [SD] 9.95) in the control group and $27.54{\times}10^{-5}U/mg$ (SD 31.81) in the experimental group. The difference between these means was not statistically significantly (p = 0.778), and the distribution of the AST values was also similar in both groups. Conclusions: No statistically significant increase in AST activity in the pulp of mechanically loaded teeth was detected after 6 months of orthodontic alignment, as compared to that of teeth extracted from individuals who had not undergone orthodontic treatment. This suggests that time-related regenerative processes occur in the dental pulp.