• Journal of the East Asian Society of Dietary Life
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• v.1 no.3
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• pp.299-304
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• 1991

In this study the effects of water extracts of endocarps and seeds of omija(Schizandra chinensis Baillon)on alcohol metabolism in rats were investigated. 25% alcoholic solution(v/v,0.75g/200g B.W.)and 40% alcoholic solution(v/v,0.80g/200g B.W.)were orally administered to rats for 2 hours. The levels of metabolites and enzyme activities both on serum and liver were not changed by acute oral adminiatration of 25% and 40% alcoholic solution. Blood alcohol levels were significantly lowered by treatment of water extracts of endocarps and seeds of omija in rats administered with 25% and 40% alcohol. In 25% alcohol treated group, serum GPT level was decreased but hepatic G-6-P DH and pyruvate levels were increased. In 40% alcohol treated group, water extracts of endocarps and seeds of omija resulted in a significant decreased in serum levels of FFA, GPT but increased in serum glucose level. Hepatic levels of cytosolic protein, glycogen and pyruvate were increased by water extracts of omija parts in 40% alcohol treated group.

• BMB Reports
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• v.30 no.3
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• pp.182-187
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• 1997

The NADPH oxidase of phagocytes catalyzes the reduction of oxygen to $O_2^-$ at the expense of NADPH. The enzyme is dormant in resting neutrophils and becomes activated on stimulation. During activation, $p47^{phox}\;(\underline{ph}agocyte\;\underline{ox}idase\;factor)$, a cytosolic oxidase subunit, becomes extensively phosphorylated at a number of serines located between S303-S379. Oxidase activation can also be achieved by the addition of phosphorylated recombinant $p47^{phox}$ by protein kinase C in the cell-free system in the presence of $GTP{\gamma}S$. The cell-free activation is inhibited by wortmannin and LY294002. specific inhibitors of phosphatidylinositol 3kinase (PI 3-kinasel) These results indicate that PI 3-kinase may playa pivotal role in the activation of NADPH oxidase.

• Biomedical Science Letters
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• v.11 no.4
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• pp.473-479
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• 2005

Possible mechanism of decreased catechol-O-methyltransferase (COMT) activity in cholestatic rat liver was studied. Hepatic and serum COMT activities were determined from the experimental rats with common bile duct ligation (CBDL). The Michaelis-Menten constants in this hepatic enzyme were also measured. The activities of cytosolic, mitochondrial and mircosomal COMT as well as their Vmax values were found to be decreased significantly in CBDL plus taurocholic acid (TCA) injected group than in the control group, such as CBDL alone groups. However, their Km values in the experimental groups did not vary. Serum COMT activity increased slightly in the CBDL plus TCA injected group than in the control group. The above results suggest that TCA represses biosynthesis of the COMT in the liver. The elevated activity of the serum COMT is believed to be caused by the increment of membrane permeability of hepatocytes upon TCA mediated liver cell necrosis.

• Natural Product Sciences
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• v.1 no.1
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• pp.55-60
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• 1995

In the course of evaluation of hepatoprotective components against alcohol-induced toxicity from Aloe spp., the methanol extract was found to cause a significant inhibition of rat liver cytosolic alcohol dehydrogenase activity. Systematic fractionation of active tractions monitored by bioassay led to isolation of four compounds; aloe-emodin, aloenin, ethylidene-aloenin and ${\beta}-sitosterol$, which were estimated as active principles for inhibition of c-ADH and c-ALDH activities in vitro.

• BMB Reports
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• v.32 no.6
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• pp.535-540
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• 1999

Two types of the thioltransferase (also called glutaredoxin) have been previously detected in the cytosolic extract of Schizosaccharomyces pombe, a fission yeast. Previously, the one with a smaller molecular mass (14kDa) was purified and characterized. In the present study, the second thioltransferase was purified. The purification procedure included ammonium sulfate fractionation (40-80%), Sephadex G-200 gel filtration, DEAE-cellulose ion-exchange chromatography, Sephadex G-50 gel filtration, and glutathione-agarose affinity chromatography. The purified enzyme showed a single band on SDS-PAGE, and its molecular mass was determined to be 23 kDa. It utilizes various compounds as substrates, including 2-hydroxyethyl disulfide. Interestingly, we found that the purified thioltransferase also contains significant glutathione S-transferase activity.

• Journal of Plant Biology
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• v.32 no.4
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• pp.285-292
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• 1989

The intracellular localizations of polyamines and their related enzymes were investigated from young spinach leaves. Polyamines were present in all parts of plant cells, both in the subcellular organelles and in the soluble fraction of cytoplasm, however, polyamines were mainly located in the cytosolic fraction. Most activities of L-arginine decarboxylase(ADC) and L-ornithine decarboxylase(ODC), two important enzymes of putrescine and polyamine biosynthesis, were detected in cytosol fraction, while in subcellular organelles the activities were very low. Activities of diamine oxidase(DAO) and polyamine oxidase(PAO), the catabolic enzyme of diamine and polyamine, were not detected in spinach leaves. It was suggested that polyamines and their related synthetic enzymes were located in the soluble fraction of cytoplasm.

• Archives of Pharmacal Research
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• v.17 no.5
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• pp.354-359
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• 1994

The activity of SD-framesylcysteine O-methyltransferase was assayed by incubating the enzyrne with a synthetic in vitro substrate, [N-acetyl-S-trans, trns-famesyl-L-cysteine (AFC)], together with S-adenosyl-L-[emthyl-$_{14}$C)ester(AFCME)], was then analyzed either directly on HPLC or by converting the AFC[$methyl^{14}C$]ME to [$methyl^{14}C$] aclcohol by basehydrolysis. Employing these two analytical methods, it was established that a peptide purifed from rat liver cytosol fraction [Int. J. Biochem., 25, 1157 919930] strongly inhibited the above enzyme activity with $IC_{50}\; of\; 7.1\times 10^{-8}$ M. Also, the S-famesylcysteine O-methyltransferase from several human colon cancer cells was equally inhibited by the peptide.

• Fisheries and Aquatic Sciences
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• v.11 no.3
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• pp.177-181
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• 2008

Glyceraldehyde 3-phosphate dehydrogenase(GAPDH) is a key enzyme for carbohydrate metabolism in most living organisms. Recent reports and our own searches of teleost species in publicly available genomic databases have identified at least two distinct GAPDH genes in a given species. The two GAPDH genes are located on the same chromosome in teleosts, whereas they are located on the different chromosomes in mammals. Thus, we reconstructed a phylogenetic tree to better understand the evolutionary history of the GAPDH genes in the vertebrate lineage. Our phylogenetic analysis revealed unambiguously that the two GAPDH genes of teleosts are phylogenetically closely affiliated to one of the cytosolic GAPDH and spermatogenic GAPDH-S of mammals. This indicates that the two paralogous GAPDH genes shared a common ancestor and subsequently underwent a gene duplication event during early vertebrate evolution. However, GAPDH-S of teleosts showed significant differences in the polypeptide residues and tissue distribution of its mRNA transcripts from that of mammals, implying they have undergone a different history of functionalization.

• Natural Product Sciences
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• v.9 no.3
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• pp.170-173
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• 2003

The anti-oxidant activities of decursinol angelate (1) and decursin (2) isolated from Angelica gigas were investigated. These two coumarins exhibited decrease in serum transaminase activities elevated by hepatic damage induced by $CCl_4-intoxication$ in rats. They also showed increase in anti-oxidant enzyme such as hepatic cytosolic superoxide dismutase (SOD), catalase, and glutathione peroxidase (GSH-px) in $CCl_4-intoxicated$ rats. These results suggest that decursinol angelate (1) and decursin (2) from A. gigas possess not only the anti-oxidant, but also the hepatoprotective activities in rats.

• Herbal Formula Science
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• v.10 no.2
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• pp.85-95
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• 2002

Objectives: In traditional medicine, Wolgukwhan has been used for the treatment of digestive system disease, such as indigestion, brash, ructation, nausea and vomiting. This study was purposed to investigate the effects of Wolgukwhan methnol extract (WGWM) on oxidative liver cell injury. Methods: In vivo assay, we administerated acetaminophen(500mg/kg, i.p.) to starved mice 24hrs after pretreatment of WGWM for 6days. In the liver homogenates, lipid peroxide and glutathione(GSH) levels were measured. In addition, activities of hepatic enzyme, such as catalase, glutathione peroxidase(GPX), glutathione S-transferase(GST) were measured in the hepatic mitochondrial and cytosolic fractions. Results: In vivo administeration of WGWM showed effective inhibition of acetaminophen induced lipid peroxidation and elevations of glutathione level. The acetaminophen treatment resulted in a decrease of catalase, GPX and GST activities. By contrast, WGWM pretreatment increased compare to those of untreated groups. Conclusions: These results suggested that WGWM might protect against lipid peroxidation by free radicals, destruction of hepatic cell membranes.