• Parasites, Hosts and Diseases
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• 제21권1호
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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.

• 한국임상약학회지
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• 제3권1호
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• pp.45-53
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• 1993

Biphenyl Dimethyl dicarboxylate(DDB) has been regarded as a safe, effective drug for decreasing serum aminotransferase levels from elevated serum aminotransferase levels, which cause acute or chronic hepatitis and chronic liver diseases. This study was designed to low dose(22.5mg/day) & short-term therapy effectiveness for 4 weeks of DDB in 30 chronic hepatitis patients with elevated serum aminotransferases. The following results were observed. 1. Serum alanine aminotransferase(ALT) levels significantly decresed from 173. $97\pm130.62(U/L)$ of pretreatment level to $32.23\pm19.22(U/L)$ after treatment for 4 weeks(p<0.00l) and normalized patients by $73\%$ 2. Serum aspartate (AST) aminotransferase levels significantly decreased from $94.90\pm49.17(U/L)$ of pretreatment level to $45.30\pm23.25(U/L)4 after treatment(p0<0.01). 3. However, no significant effects in the serum AST & ALT changes by which cause hepatitis and hepatitis duration (p>0.05). 4. No significant adverse effects were observed except for mild epigastric discomfort in one patient during DDB treatment It is suggested that DDB small dosage administration can result effectively decreasing serum aminotransferase levels from chronic hepatitis patients with elevated serum aminotransferase levels.

• Fisheries and Aquatic Sciences
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• 제4권1호
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• pp.25-31
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• 2001

4-Aminobutyrate aminotransferase plays an essential role in the 4-aminobutyric acid shunt, converting 4-aminobutyrate to succinic semi aldehyde. We isolated and sequenced' a fish cDNA fragment that encodes 4-aminobutyrate aminotransferase. A brain cDNA library from flounder (Paralichthys olivaceus) was constructed using the ZAP- III XR vector and screened for the fish 4-aminobutyrate aminotransferase gene using a probe derived from the conserved sequences of known mammalian 4-aminobutyrate aminotransferases. A partial cDNA for 4-aminobutyrate aminotransferase was cloned and found to be 700 bp in length corresponding to 66 amino acids. Nucleotide sequence of the clone was aligned with NCBI (National Center for Biotechnology Information) DNA sequence data base. The result showed high sequence identity with previously reported mammalian 4-aminobutyrate aminotransferases. The trans­criptional level of flounder 4-aminobutyrate aminotransferase was detected with the presence of mRNA at different flounder tissues by reverse transcription-polymerase chain reaction (RT-PCR). The expression of flounder 4-aminobutyrate aminotransferase was also tested and detected from the flounder tissues of the brain, liver, kidney and pancreas.

• 대한임상검사과학회지
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• 제53권3호
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• pp.241-248
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• 2021

본 연구는 고혈압이 있는 대한민국 성인에서 아스파르트산 아미노전이효소(aspartate aminotransferase, AST)/알라닌 아미노전이효소(alanine aminotransferase, ALT) 비율과 맥압(pulse pressure, PP) 사이의 관계를 평가하기 위해 수행되었다. 제6차 국민건강영양조사(KNHANES VI-3, 2015)에서 성인 1,515명의 데이터를 분석했다. 본 연구에서는 몇 가지 중요한 결과가 있다. 첫째, AST (odds ratio [OR], 1.018; 95% confidence interval [CI], 1.002~1.033), ALT (OR, 0.982; 95% CI, 0.969~0.996) 및 AST/ALT ratio (OR, 1.367; 95% CI, 1.027~1.819)는 고PP 결정하는 독립적인 요인이었다. 둘째, 관련변수(연령, 성별, 흡연, 음주, 규칙적인 운동, TC, TG, HDL-C, FBG, BMI, WC)를 조정한 후의 결과에서 AST/ALT ratio의 1 사분위에 대한 고PP의 OR을 기준으로, AST/ALT ratio의 2 사분위(OR, 1.188; 95% CI, 0.817~1.727) 및 AST/ALT ratio의 3 사분위(OR, 1.169; 95% CI, 0.800~1.710)는 유의하지 않았지만, AST/ALT ratio의 4 사분위(OR, 1.632, 95% CI, 1.113~2.393)에서 유의하게 높았다. 결론적으로, 고혈압이 있는 대한민국 성인에서 고PP은 AST/ALT ratio 및 AST와 양의 상관관계가 있었지만 ALT와 음의 상관계가 있었다.

• 대한한방내과학회지
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• 제21권2호
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• pp.337-339
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• 2000

Indigestion is one of the most frequent symptom in chronic hepatitis. We treated a 20 year-old female patient of chronic active hepatitis type B with Sengangeonbi-tang. The patient complained indigestion and constipation. The serum aminotransferase were higher and viral marker showed hepatitis was in active phase. 1 week later, the symptom had been changed from severe to mild and aminotransferase decreased. We continued to prescribe the medicine 2 weeks more and could observe that the symptom disappeared and the aminotransferase fell down under normal value with no side effect. Sengangeonbi-tang showed desirable effect on indigestion and more rapid recovery of aminotransferase than previous reports about treating hepatitis.

• Advances in Traditional Medicine
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• 제3권1호
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• pp.18-20
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• 2003

The purpose of this study was to examine the effect of supplementary highly purified chitosan (HPC) on blood alcohol concentration in healthy human. The human study was performed with two sections. Each section of the study was conducted by two-phase cross-over design with a week wash-out period. All volunteers took HPC in one phase, and took a placebo in the next phase. Blood alcohol concentrations were different between in those taking HPC and in those taking the placebo in the human. And the concentration of serum aspartate aminotransferase (AST, GOT) and alanine aminotransferase (ALT, GPT), the indicator of liver cell damage, was lowered in those taking HPC, compared to those taking the placebo. In conclusion, taking HPC prior to drinking alcohol can somewhat reduce alcohol concentration in human blood and liver cell damage.

• Pediatric Gastroenterology, Hepatology & Nutrition
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• 제16권2호
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• pp.89-94
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• 2013

Purpose: The aim of this study was to evaluate the prevalence of increased aminotransferase levels and to identify associated factors in children admitted to hospital with urinary tract infections (UTIs). Methods: The study included children with a diagnosis of UTI who were admitted to the Konyang University Hospital from January 2007 to May 2011. The total number of patients was 249 and the mean age was $15.88{\pm}28.21$ months. UTI was defined as a positive urine culture (> $10^5$/colony forming unit [CFU]) with pyrexia. Patients were treated by intravenous antibiotics, such as ampicillin/sulbactam, aminoglycoside, cephalosporins or vancomycin. Patients with neonatal jaundice or other liver disease were excluded. We investigated the relationship of aminotransferase levels with the type of antibiotic, degree of vesicoureteral reflux (VUR), and causative organisms. Results: Children with increased aminotransferase levels were younger than those with normal levels (p=0.001), but white blood cell count, platelet count, causative organisms, type of antibiotics and presence of VUR were not associated with aminotransferase levels. Aminotransferase levels became normal within 1 month after discharge without special measures, except in 1 case. Conclusion: We found that many children with UTI have abnormal aminotransferase levels. In most cases, this change is mild and self-limiting. We conclude that increased aminotransferase level increase during UTI do not require unnecessary tests and excessive treatment.

• Journal of Microbiology and Biotechnology
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• 제21권10호
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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.

• Journal of Microbiology and Biotechnology
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• 제18권1호
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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.

• BMB Reports
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• 제32권2호
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• pp.181-188
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• 1999

4-Aminobutyrate aminotransferase plays an essential role in the 4-aminobutyric acid shunt, converting 4-aminobutyrate to succinic semialdehyde. Recombinant 4-aminobutyrate aminotransferases were overexpressed as their catalytically active forms in E. coli by coproduction with thioredoxin and their solubilities were also dramatically increased. In order to study the structural and functional aspects of the C-terminal domain of brain 4-aminobutyrate aminotransferase, we have constructed a C-terminal mutant of pig brain 4-aminobutyrate aminotransferase and analyzed the functional and structural roles of C-terminal amino acids residues on the enzyme. The deletion of five amino-acid residues from C-terminus did not interfere with the kinetic parameters and functional properties of the enzyme. Also, the deletion did not affect the dimeric structure of the protein aligned along the subunit interface at neutral pH. However, the deletion of the C-terminal region of the protein changed the stability of its dimeric structure at acidic pH. The dissociation of the enzyme acidic, facilitated by the deletion of five amino acids from C-terminus, abolished the catalytic activity.