• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.5
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• pp.651-657
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• 1995

The antioxidative activity of each fraction in human milk was examined using H2O2 and FeSO4-induced lipid peroxidation of mouse liver homogenate in order to elucidate the antioxidative substances of human milk. High molecular weight(~>20KD) fraction had more antioxidative effect on lipid peroxidation than low molecular weight(~ <20KD) fraction. Furthermore, the changes of antioxidative enzyme activities were estimated during lactation to study the roles of human milk. The human milk showed high activities of catalase, glutathione(GSH) peroxidase and GSH S-transferase. These results suggest that the antioxidative activities may mostly be attributed to high molecular weight fraction containing catalase, GSH peroxidase and GSH S-transferase.

• Korean Journal of Environmental Agriculture
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• v.16 no.4
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• pp.365-372
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• 1997

Biochemical characteristics and activities of glutathione-S-transferases(GSTs) and carboxylesterase extracted from soybean and corn plants treated with quizalofop-ethyl were investigated. Km value and Vmax of GSTs extracted from soybean and corn plants were $6.7{\times}10^{-3}M$ nmole/mg/min, 50, 20 nmole/mg/min, respectively. Optimum pH of carboxylesterase from soybean and corn was 7.0. Km value and Vmax of carboxylesterase extracted from soybean and corn plants were $4.2{\times}10^{-4}M$, $2.5{\times}10^{-4}M$ nmole/mg/min, 33, 10 nmole/mg/min, respectively. GSTs and carboxylesterase activity were reduced by quizalofop-ethyl. GSTs and carboxylesterse activity of corn was more reduced than that of soybean. When soybean and corn were treated by 80 ppm of quizalofopethyl. Soybean recovered after 10 days elapsing, but corn withered after 3days elapsing.

• BMB Reports
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• v.29 no.5
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• pp.462-467
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• 1996

Acetolactate synthase (ALS, EC 4.1.3.18) is the first common enzyme in the biosynthesis of leucine, isoleucine, and valine. It is the target enzyme for several classes of herbicides, including the sulfonylureas, the imidazolinones, the mazolopyrimidines, the pyrimidyl-oxy-benzoates, the pyrimidyl-thio-benzens, and the 4,6-dimethoxypyrimidines. An amino-terminal fragment of the sulfonylurea-resistant ALS gene (SurB) from Nicotiana tabaccum was cloned into the bacterial expression vector pGEX-2T. The resulting recombinant plasmid pGEX-ALS1 was used to transform Escherichia coli strain BL21, and the tobacco ALS was expressed in the bacteria as a protein fused with glutathione S-transferase (GST). Polyclonal antibodies against the fusion product (GST-ALS) were produced, and the sensitivity of GST-ALS with the rabbit anti-GST-ALS IgG was up to 50 ng. This antibody was used for Western blot analysis of the partially purified ALS from barley shoots. The results suggest that the polyclonal antibody produced in this study can be used to detect plant ALS.

• Journal of Embryo Transfer
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• v.25 no.4
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• pp.273-279
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• 2010

Follicular cystic follicles (FCFs) show delayed regression with persistent follicle growth. However, the mechanism by which follicles are persistently grown remains unclear. Glutathione S-transferases (GSTs) are drug-metabolizing and detoxification enzymes that are involved in the intracellular transport and metabolism of steroid hormones. In this study, a proteomic analysis was performed to identify whether GST expression is changed in bovine FCFs and to predict the interactions between GST and other proteins. Normal follicles and FCFs were classified based on their sizes (5 to 10 mm and 25 mm). In bovine follicles, GST mu 1 (GSTM1) was detected as a differentially expressed protein (DEP) and significantly up-regulated in FCFs compared to normal follicles (p<0.05). Consistent with the proteomic results, semi-quantitative PCR data and western blot analysis revealed an up-regulation of GSTM1 in FCFs. Expression levels of aromatase and dehydrogenase proteins were changed in FCFs. These results show that the up-regulation of GSTM1 that is observed in bovine FCFs is likely to be responsible for the persistent follicle growth in FCFs as the activity of aromatase and the dehydrogenases.

• Animal cells and systems
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• v.12 no.3
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• pp.149-155
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• 2008

We have isolated and characterized Agrius convolvuli cDNA encoding a c-type lysozyme. The cDNA sequence encodes a processed protein of 139 amino acid residues with 19 amino acid residues amino-terminal signal sequence and 120 amino acid residues mature sequence. The amino acid residues responsible for the catalytic activity and the binding of the substrate are conserved. Agrius lysozyme has a high identity to Manduca sexta. Recombinant A. convolvuli lysozyme was expressed in Escherichia coli BL21(DE3) pLysS cells for pGEX 4T-1 expression vector. Their optimal conditions for the fusion protein expression and purification were screened. Lysozyme gene amplified with primers ACLyz BamHI and ACLyz XhoI was ligated into the pGEX 4T-1 vector, which contained the glutathione S-transferase(GST) gene for fusion partner. The fusion protein was induced by IPTG and identified by SDS-PAGE analysis. Molecular weight of the fusion protein was estimated to be about 45 kDa. Recombinant lysozyme, fused to GST, was purified by glutathion-Sepharose 4B affinity chromatography. Western blot analysis of this protein revealed an immunoreactivity with the anti-Agrius lysozyme.

• Journal of Life Science
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• v.14 no.1
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• pp.148-153
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• 2004

In this study, we investigated the effect of water, extract of Terminalia Chebula (TC) on physiological activity in mice. TC water extract showed hemagglutination against several different types of red blood cells. $LD_{50}$ of TC extract was 390 mg/kg (po). Treatment of TC water extract orally administered 200, 300 mg/kg daily for one week. Hepatic cytosolic enzymes, xanthine oxidase and aldehyde oxidase activities were significantly increased comparison with normal group. Treatment of TC water extract increased hepatic malondialdehyde (MDA) formation, and reduced glutathione content. We also found that the decreased activities of glutathione S-transferase and glutathione reductase but was not affected activities of $\gamma$-glutamylcysteine synthetase after treatment of TC water extract. These results suggested that increase of the hepatic lipid peroxide is caused by glutathione reduction.

• Journal of Ginseng Research
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• v.22 no.4
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• pp.267-273
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• 1998

Pretreatment of acidic polysaccharide of Korean red ginseng (AcPS) for two weeks remarkably lowered the elevated content of lipid peroxide and levels of aminotransferases, sorbitol dehydrogenase, ${\gamma}$-glutamyltransferase, alkaline phosphatase and lactate dehydrogenase in liver intoxicated by acetaminophen (AA) . Pretreatments of AcPS also strengthen the liver function of glutathione related detoxication system indicated by glutathione contents and activities of glutathione S-transferase and glutathione reeducates which were affected by AA treatments. Activity of ${\gamma}$-glutamylcysteine syntheses was not changed by AcPS pretreatment whereas the activity of flu tathione reeducates was increased significantly. These results collectively indicate that the treatments of AcPS can promote the metabolism of lipid and reduce the production of peroxide in acetaminophen-intoxicated animals.

• Environmental Analysis Health and Toxicology
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• v.22 no.1 s.56
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• pp.9-17
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• 2007

Hermansky-Pudlak Syndrome (HPS) 환자에서 조기에 발생되는 폐섬유화의 원인을 알아보고자, 생쥐 HPS 모델인 ep/ep,pe/pe 돌연변이종의 폐 항산화계의 환성과 방사선에 대한 반응을 측정하였다. HPS 폐에서는 대조군에 비해 glutathione이 더 산화되어 있었고, catalase, glutathione S-transferase(GST) 등의 항산화효소의 활성이 저하되어 있었으며, 10 Gy의 방사선을 조사하였을 때, glutathione 양이 감소하였고, 대조군 폐에서 보여지는 방사선에 의한 ${\gamma}$-glutamylcysteine ligase(GCL), glutathione peroxidase(GPx) 활성의 유의성 있는 증가가 관찰되지 않았다. 이 결과로부터 HPS 환자의 폐는 항산화계 활성이 저하되어 있을 뿐 아니라, 산화적 스트레스가 가해 졌을 때 적응 반응이 매우 취약하여 산화적 환경에 노출된 폐의 병증을 유발할 수 있음을 추측할 수 있다.

• Analytical Science and Technology
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• v.22 no.3
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• pp.228-234
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• 2009

To gain further insight into herbicide detoxification of plant, we purified a glutathione S-transferase from Brassica oleracea (BoGST) and studied its substrate specificity towards several xenobiotic compounds. The BoGST was purified to electrophoretic homogeneity with approximately 10% activity yield by DEAE-Sephacel and GSHSepharose column chromatography. The molecular weight of the BoGST was determined to be approximately 23,000 by SDS-polyacrylamide gel electrophoresis and 48,000 by gel chromatography, indicating a homodimeric structure. The activity of the BoGST was significantly inhibited by S-hexyl-GSH and S-(2,4-dinitrophenyl)GSH. The substrate specificity of the BoGST displayed high activities towards CDNB, a general GST substrate and ethacrynic acid. It also exhibited GSH peroxidase activity toward cumene hydroperoxide.

• Journal of the Korean Society of Food Science and Nutrition
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• v.36 no.6
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• pp.708-719
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• 2007

Glutathione S-transferase genotypes GSTT1, GSTM1 and GSTP1 were characterized in 104 healthy male and female subjects and compared with parameters of oxidative stress at the level of DNA and lipids, with antioxidant enzymes, and with plasma antioxidants in smokers and non.smokers. Of the 104 subjects studied, 57.4% were GSTT1 present and 47.6% were GSTM1 present. The GSTP1 polymorphisms a and b were represented as follows: a/a, 75.5%; a/b, 21.6%; b/b type, 2.9%. The GSTT1 null genotype was associated with decreased glutathione in erythrocytes and elevated lymphocytes DNA damage. GST-Px was higher in GSTT1 null compared with GSTT1 present type. The homozygous GSTP1 genotype was not associated with any antioxidant status or DNA damage. The difference in plasma ${\alpha}$-carotene and erythrocytes GSH-Px and GST activities between smokers and non-smokers was detected in the GSTT1 null genotype. Plasma ${\gamma}$-tocopherol and ${\beta}$-carotene decreased significantly in smokers having GSTM1 null genotype. When GSTT1 and GSTM1 were combined, plasma lycopene and erythrocyte GST were reduced in smokers in both null types of these genes. As for GSTP1 genotype, plasma ${\alpha}$-carotene and erythrocytes GSH-Px decreased significantly in smokers with GSTP1 b/b, while erythrocytes GSH-Px activities decreased in smokers with GSTP1 a/b. The different ${\beta}$-carotene level between smokers and non-smokers was seen with both GSTP1 a/a and a/b genotype. It seems that polymorphisms in the phase II metabolizing enzyme glutathione S-transferase may be important determinants of commonly measured biomarkers.