• 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.

• Journal of Microbiology and Biotechnology
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• v.18 no.1
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• pp.48-54
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• 2008

A putative ${\omega}$-aminotransferase gene, cc3143 (aptA), from Caulobacter crescentus was screened by bioinformatical tools and overexpressed in E. coli, and the substrate specificity of the ${\omega}$-aminotransferase was investigated. AptA showed high activity for short-chain ${\beta}$-amino acids. It showed the highest activity for 3-amino-n-butyric acid. It showed higher activity toward aromatic amines than aliphatic amines. The 3D model of the ${\omega}$-aminotransferase was constructed by homology modeling using a dialkylglycine decarboxylase (PDB ID: 1DGE) as a template. Then, the ${\omega}$-aminotransferase was rationally redesigned to increase the activity for 3-amino-3-phenylpropionic acid. The mutants N285A and V227G increased the relative activity for 3-amino-3-phenylpropionic acid to 3-amino-n-butyric acid by 11-fold and 3-fold, respectively, over that of wild type.

• Microbiology and Biotechnology Letters
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• v.27 no.3
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• pp.184-190
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• 1999

To acquire an industrially useful biocatalyst for the enzymatic synthesis and production of various D-amino acid aminotransferase (D-AAT) activity. The enzyme activity was found from 110 strains of isolated thermophiles revealing its wide occurrence in thermophiles. Enzyme activity and thermal stability of the D-AAT producers were compared. Finally we have selected four thermophiles as producers of potent biocatalysts for the D-amino acid production; two thermophiles, Bacillus sp. Lk-1 and LK-2, having higher specific activity and two thermophiles, B. stearothermophilus KL-01 and Bacillus sp. KLS-01, having higher thermal stability than the D-AAT producers. Taxonomic and physiological characteristics of the four isolated thermophiles were described herein.

• Parasites, Hosts and Diseases
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• v.21 no.1
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• pp.49-57
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• 1983

The distribution and Properties of branched chain amino acid aminotransferase (EC 2.6. 1.42) was investigated in adult Fasciola hepatica. Fascicla hepatica was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of branched chain amino acid aminotransferase was measured by the method of Ichihara and Koyama (1966) . Isozyme patterns of this enzyule was also examined by DEAE-cellulose column chromatography. The results obtained were as follows; 1. The activity in homogenate was found to be 12.69 units/g wet tissue. The activity of this enzyme was relatively high compared with those in rat tissues. 2. The distribution of branched chain amino acid aminotransferase in the subcellular organelles showed that 87.8% of the activity was in cytosolic, 10.9% in mitochondrial and 1.3% was in nuclear fraction. 3. Cytosolic fraction of Fasciola hepatica contained Enzyme I, but not Enzyme II and III, of branched chain amino acid aminotransferase. Ensyme I was eluted by 50mM phosphate buffier from DEAE-cellulose column and catalyzed the transamination of all three branched chain amino acids. 4. The Enzyme I was purified about 22-folds increase in specific activity after chromatography on DEAE-cellulose. 5. The best substrate among three amino acids (leucine, isoleucine and valise) was L-isoleucine. 6. The optimal temperature of Enzyme I was $45^{\circ}C$ and the optimal pH was 8.2. 7. The Km value for leucine of Enzyme I was 4.17 mM. 8. The Km values for a-ketoglutarate and pyridoxal phosphate of Enzyme I were 0.41mM and $4.76{\times}10^{-3}{\;}mM$, respectively.

• 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.

• Archives of Pharmacal Research
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• v.14 no.1
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• pp.81-86
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• 1991

Dry powder and different extracts of Agave lophantha were tested against Biomphalaria alexandrina. The results showed that the butanol extract has high molluscicidal activity. The activity of the dry powder has been found to be stable under the effect of some simulated field conditions. Also the toxicological effect of the plant on mice was tested through determination of certain parameters such as total protein, aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase and acid phosphatase enzymes as well as histopathological study on liver and kidney.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.12 no.5
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• pp.728-734
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• 1999

Thirty new born crossbred (Bos taurus${\times}$Bos indicus) calves, divided randomly in a $3{\times}2$ factorial design, were fed calf starters containing one of three protein sources i.e., groundnut cake (GN), cottonseed meal (CS) and meat and bone meal (MB) along with either raw (M) or gelatinized maize (MG) for 90d. Milk was fed upto 56d of age. Green oats and respective calf starters were offered from 14d of age onwards ad lib. Clinical profile of serum suggested significantly (p<0.05) higher albumin and lower alanine aminotransferase activity due to CS feeding. Alklaine phosphatase activity varied significantly (p<0.05) among dietary treatments showing interaction between protein and starch sources. Inclusion of gelatinized maize resulted in significantly higher concentration of serum globulin (p<0.05) and alkaline phosphatase activity (p<0.01). reduced (p<0.05) ruminal pH was accompanied by a significant decrease (p<0.01) in $NH_3-N$ concentration in the strained rumen liquor (SRL) of MG fed calves. Ruminal amylase activity was lower (p<0.05) on MG diets. Alanine aminotransferase activity in the rumen exhibited a significant (p<0.01) interaction between protein and starch sources. While feeding of CS significantly (p<0.01) reduced alanine aminotransferase activity, inclusion of thermally processed maize reduced (p<0.01) both aspartate and alanine aminotransferase activities in the rumen. The overall blood picture was similar among treatments, whereas rumen metabolites especially enzyme activities, seems to be altered with source of degradable protein an starch.

• 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.