• The Journal of Korean Medicine
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• v.24 no.3
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• pp.96-107
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• 2003

Objective : This study was undertaken to determine if Pyunggangaeuljihyul-tang (Pinggankaiyuzhixue-tang, PG) has a protective effect against cell injury induced by various toxic agents in rabbit liver, Methods : Cell injury in vitro was estimated by measuring lactate dehydrogenase (LDH), and that in vivo was estimated by measuring alanine aminotransferase (ALT) and aspartate aminotransferase (AST) activity in serum. Lipid peroxidation was examined by measuring malondialdehyde, a product of lipid per oxidation. Results : PG prevented the LDH release by $CCl_4$, mercury, menadione, and tert-butyl hydroperoxide treatment in vitro in liver slices. The extent of protection by 2% PG was similar to that of $10{\mu\textrm{M}}$ N,N'-diphenyl-p-phenylenedianline, a potent antioxidant, in tert-butyl hydroperoxide-induced LDH release. PG also prevented lipid peroxidation and depletion of cellular ATP induced by Hg. Hg causes motphological changes including cell necrosis and its effect was significantly prevented by PG. When rats were treated intraperitoneatly with 0.5 ml/kg of $CCl_4$, serum alanine aminotransferase and aspartate aminotransferase activities were increased compared with the control, which was significantly inhibited by pretreatment of PG. PG also prevented reduction in GSH and lipid peroxidation induced by $CCl_4$ Conclusion : These results suggest that PG exerts aprotective effect against various toxic agents by its antioxidant action in liver tissues. Thus, PG may be used in prevention and treatment of drug-induced liver cell injury. However, the precise mechanisms of PG protection remain to be determined.

• Journal of radiological science and technology
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• v.16 no.2
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• pp.87-94
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• 1993

In order to investigate radiation effects on the liver, functional changes of liver were analyzed after irradiation. Doses of 10 Gy, 15 Gy and 20 Gy were exposed partially to the liver of male rats(Sprague-Dawley) with X-ray(4MV linear accelerator) at room temperature. On 1, 2, 4 and 8 weeks after irradiation, liver tissues and sera of the animals were compared with those of unirradiated animal by liver function tests. Enzyme activities in sera such as alanine aminotransferase, aspartate aminotransferase, malondialdehyde. The content of malondialdehyde in the activities of many enzymes including alanine aminotransferase, aspartate aminotransferase in sera were increased slightly with increasing exposure dose in all experiments and the activities of these enzymes increased markedly in 20 Gy irradiated groups. From these above results, functional changes of the liver were induced in all irradiated groups. Damaged liver was recovered along with time collapse after irradiation to the doses of 10 Gy and 15 Gy while no recovery was deteced within 8 weeks after irradiation to 20 Gy. These results suggest that careful attention must be paid to liver not to be included in exposure field in radiation therapy.

• Korean Journal of Clinical Laboratory Science
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• v.43 no.1
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• pp.6-11
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• 2011

In clinical chemistry tests, the interfering substances such as hemoglobin, lipid, bilirubin, and drugs, etc. can cause the changes of test results performed by spectrophotometrical methods. We evaluated the effects of interfering substances on the test results by adding interfering substances on the samples in the 19 kinds of clinical chemistry tests such as aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, lactate dehydrogenase, gamma-glutamyltransferase, total protein, albumin, glucose, total cholesterol, total bilirubin, triglyceride, uric acid, calcium, inorganic phosphours, high density lipoprotein cholesterol, low density lipoprotein cholesterol, creatinine, blood urea nitrogen, and C-reactive protein using newly implemented automatic chemical analyzer Toshiba TBA-C8000 under the direction of CLSI EP07-A guideline. Hemolytic samples show increased concentration of total protein, aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase and reduced concentration of total bilirubin, alkaline phosphatase by interfering effect. Hyperlipemic samples show increased concentration of total protein and alkaline phosphatase and reduced concentration of low density lipoprotein cholesterol. The samples with conjugated bilirubinemia show increased concentration of inorganic phosphours, otherwise the samples with unconjugated bilirubinemia show no interference or allowable range in the test result.

• BMB Reports
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• v.35 no.2
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• pp.220-227
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• 2002

Two aspartate aminoransferase (EC 2.6.1.1) isoenzymes (AAT-1 and AAT-2) from Lupinus albus L. cv Estoril were separated, purified, and characterized. The molecular weight, pI value, optimum pH, optimum temperature, and thermodynamic parameters for thermal inactivation of both isoenzymes were obtained. Studies of the kinetic mechanism, and the kinetics of product inhibition and high substrate concentration inhibition, were performed. The effect of some divalent ions and irreversible inhibitors on both AAT isoenzymes was also studied. Native PAGE showed a higher molecular weight for AAT-2 compared with AAT-1. AAT-1 appears to be more anionic than AAT-2, which was suggested by the anion exchange chromatography. SDS-PAGE showed a similar sub-unit molecular weight for both isoenzymes. The optimum pH (between 8,0 and 9.0) and temperature ($60-65^{\circ}C$) were similar for both isoenzymes. In the temperature range of $45-65^{\circ}C$, AAT-2 has higher thermostability than AAT-1. Both isoenzymes showed a high affinity for keto-acid substrates, as well as a higher affinity to aspartate than glutamate. Manganese ions induced an increase in both AAT isoenzymes activities, but no cooperative effect was detected. Among the inhibitors tested, hydroxylamine affected both isoenzymes activity by an irreversible inhibition mechanism.

• Korean Journal of Veterinary Research
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• v.43 no.4
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• pp.641-648
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• 2003

Changes of plasma DNA contents and serum biochemical values were measured in rats administered with $HgCl_2$ to investigate the in vivo cytotoxic effects of mercury and examine the usefulness of these changes as indicators of mercury exposure and diagnosis of mercury poisoning. Rats were given once intraperitonealy $HgCl_2$(0.13. 0.32. 0.8 and 2 mg/kg b.w) and the changes of plasma DNA contents and serum biochemical values were measured at the time of 2, 4, 8, 24, 48 and 72 hours after the administration of $HgCl_2$. Plasma DNA contents began to increase from 2 hours after the administration of $HgCl_2$ in all the treatment groups significantly compared to control with dose-dependent pattern. The levels of plasma DNA reached to peak at 48 hours as 2.77, 7.60, 15.46 and 16.51 times higher than control in each treatment group of 0.13, 0.32, 0.8 and 2 mg/kgb.w, respectively and remained to be higher until 72 hours after the administration. The values of creatine kinase, aspartate aminotransferase, alanine aminotransferase, lactate dehydrogenase, blood urea nitrogen and glucose of serum were increased, however the values of alkaline phosphatase, total protein and triglyceride were decreased. These changes of increase and decrease showed dose-dependent pattern but the starting time, maintenance and magnitude of change were various and characteristic according to serum biochemical indices. Among the changes of serum biochemical values, those of aspartate aminotransferase, lactate dehydrogenase and blood urea nitrogen were apparently and significantly increased compared to control from 2 to 72 hours by the administration of 2 mg/kg $HgCl_2$. This study demonstrates that plasma DNA and serum biochemical values such as aspartate aminotransferase, lactate dehydrogenase, blood urea nitrogen and etc. are valuable as biomarkers for mercury exposure assessment and diagnosis of mercury poisoning.

• Journal of Microbiology and Biotechnology
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• v.24 no.7
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• pp.998-1003
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• 2014

Aspartate aminotransferase (AST; E.C. 2.6.1.1), a vitamin B6-dependent enzyme, preferentially promotes the mutual transformation of aspartate and ${\alpha}$-ketoglutarate to oxaloacetate and glutamate. It plays a key role in amino acid metabolism and has been widely recommended as a biomarker of liver and heart damage. Our study aimed to evaluate the extensive preparation of AST and its application in quality control in clinical laboratories. We describe a scheme to express and purify the 6His-AST fusion protein. An optimized sequence coding AST was synthesized and transformed into Escherichia coli BL21 (DE3) strain for protein expression. Ideally, the fusion protein has a volumetric productivity achieving 900 mg/l cultures. After affinity chromatography, the enzyme activity of purified AST reached 150,000 U/L. Commutability assessment between the engineered AST and standard AST from Roche suggested that the engineered AST was the better candidate for the reference material. Moreover, the AST showed high stability during long-term storage at $-20^{\circ}C$. In conclusion, the highly soluble 6His-tagged AST can become a convenient tool for supplying a much better and cheaper standard or reference material for the clinical laboratory.

• Proceedings of the Zoological Society Korea Conference
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• 1994.10a
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• pp.235.1-235
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• 1994

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.309.1-309
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• 1995

• Journal of Microbiology and Biotechnology
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• v.21 no.10
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• pp.1049-1052
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• 2011

In this study, we demonstrated the asymmetric synthesis of L-tert-leucine from trimethylpyruvate using branched-chain aminotransferase (BCAT) from Escherichia coli in the presence of L-glutamate as an amino donor. Since BCAT was severely inhibited by 2-ketoglutarate, in order to overcome this here, we developed a BCAT/aspartate aminotransferase (AspAT) and BCAT/AspAT/pyruvate decarboxylase (PDC) coupling reaction. In the BCAT/AspAT/PDC coupling reaction, 89.2 mM L-tert-leucine (ee>99%) was asymmetrically synthesized from 100 mM trimethylpyruvate.

• Korean Journal of Microbiology
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• v.25 no.3
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• pp.189-197
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• 1987

The aim of the present study was to investigate the effect of glutamate on the biosynthesis of tylosin. Activities of enzymes involved in the metabolic pathway of glutamate to form tylactone, an essential precursor of tylosin, were determined using Streptomyces fradiae grown at different concentration of glutamate. As results, it was found that cell growth and tylactone formation was controlled by the metabolic flux of oxaloacetate. It was clear that cell growth was favored by the activities of citrate synthase and aspartate aminotransferase, while the tylactone synthesis was stimulated by the activity of methylmalonyl-CoA carboxyltransferase. Therefore it was concluded that channelling of oxaloacetate was a point for favoring either cell growth or tylosin biosynthesis.