• Title/Summary/Keyword: liver enzyme activity

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Effect of Dietary Orotic Acid on Triglyceride Metabolism in Rats and Mice (Orotic acid 유발 지방간 rat 와 mouse의 중성지질 대사)

  • 조영수;차재영
    • Journal of Life Science
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    • v.6 no.3
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    • pp.159-164
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    • 1996
  • Effects of 1% dietary orotic acid on triglyceride metabolism were examined in SD-rats and Kud: ddY mice. When rats were fed semisynthetic diet containing 1% orotic acid and n-6 polyunsaturated fatty acid (linoleic acid), the hepared diet. In contrast to rats which respond to orotic acid consumption with increases in hepatic triglyceride content, mice did not so respond. The rats-limiting step in triglyceride synthesis is catalyzed by the enzyme phosphatic acid phosphohydrolase (EC3.1.3.4) which is present in the liver cytosol and microsomes of rats fed oroic acid diet. This finding suggests that the activity of this enzyme may play a tole in the fatty liver formation in rats.

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Nutritional Value and Bioactive Properties of Enzymatic Hydrolysates prepared from the Livers of Oncorhynchus keta and Oncorhynchus gorbuscha (Pacific Salmon)

  • Yoon, Ho Dong;Karaulova, Ekaterina P.;Shulgina, Lilia V.;Yakush, Evgeni V.;Mok, Jong Soo;Lee, Su Seon;Xie, Chengliang;Kim, Jeong Gyun
    • Fisheries and Aquatic Sciences
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    • v.18 no.1
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    • pp.13-20
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    • 2015
  • Calculated chemical scores (computed in relation to the FAO/WHO reference protein) for salmon liver protein hydrolysates indicated that all amino acids (other than methionine and threonine) were present in adequate or excess quantities; thus, the raw liver material is a good source of essential amino acids. The hydrophobic amino acids contents in hydrolysates prepared from Oncorhynchus keta and O. gorbuscha were 38.4 and 39.1%, respectively. The proportion of released peptides exceeding 500 kDa was reduced when hydrolysates were treated with the commercial enzyme Alcalase, although proportions in the following MW ranges were elevated: 100-500 kDa and <50 kDa. The optimal conditions for enzymatic hydrolysis were as follows: pH 7.0, $50^{\circ}C$, and a reaction time of 1 h. Of the different proteases tested, Alcalase was the most efficient for production of salmon liver hydrolysate with the highest 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity. The hydrolysates prepared from salmon liver had a balanced amino acid composition. The liver protein hydrolysates contained low molecular weight peptides, some of which may be bio-active; this bio-active potential should be investigated. Inhibition of the DPPH radical increased with increased degree of hydrolysis (DH), regardless of protease type. DPPH radical scavenging abilities, antithrombotic effects and ${\alpha}$-glucosidase enzyme inhibition effects of O. keta liver hydrolysate increased in a dose-dependent manner. Thus, salmon liver hydrolysate may be useful in functional food applications and as a source of novel products.

Influence of Dietary Zinc, Copper and Cadmium Levels on Rat Liver Aryl Sulfotransferase IV Activity

  • Chung Keun Hee;Ringel David P.;Shin Kyung Ok
    • Nutritional Sciences
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    • v.9 no.1
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    • pp.20-28
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    • 2006
  • Aryl sulfotransferase (AST) IV is a liver enzyme involved in detoxication and has been shown to be susceptible to down regulation by a number of hepatotoxic xenobiotics. Studies presented here to investigate the ability of biological and non-biological divalent metal cations on AST IV activity showed that AST IV was strongly inhibited following in vitro or in vivo exposure to. Zn ( II ), Co ( II ) or Cd ( II ). It was found that $0.025\sim$2.5 uM of these metal ions were sufficient to cause $50\%$ of inhibition in vitro in purified AST IV and $0.25\sim$25 uM of these metal ions in liver cytosolic fractions. For the in vivo study, 1,000 mg Cu ( II )/kg, 2,000 mg Zn ( II )/kg or 250 mg Cd( II )/kg was added to individual diets and administered to three (3) group; of mts over a 7 week period The Co ( II )-supplemented diet produced no apparent change in rat growth rate and resulted in 30-fold increase in liver cytotolic Cu ( II ) levels, suggesting that elevated levels of Cu ( II ) ion in the liver were responsible for the loss of AST IV activity. In contrast, the Zn ( II )-supplemented diet caused a decrease in rat growth rates and resulted in zero increase in liver Zn ( II ) levels, which suggested an indirect inhibition mechanism was caused by Zn ( II ) in the liver. Rats were fed the Cd-supplemented diet also displayed a decrease in growth rate with little or no change in liver Cu ( II ) or Zn ( II ) levels. When the liver cytosols of mts from the metal ion diets were immunochemically analyzed for the AST IV and albumin contents, no significant changes were observed in albumin levels. However, AST IV contents in the cytosols of mts fed the Zn ( II )-supplemented diets showed a slight decrease in amount These results showed that AST IV activity in vitro and in vivo can be inhibited by Co ( II ), Zn ( II ), and Cd ( II ) by apparently different mechanisms. The immediate response to a Zn injection showed a decrease in AST IV activity but not in the AST IV content in liver cytosol. These mechanisms appeared to involve direct actions of the metal ion on AST IV activity and indirect actions affecting AST IV amount.

Anticancer Activity of Extremely Effective Recombinant L-Asparaginase from Burkholderia pseudomallei

  • Darwesh, Doaa B.;Al-Awthan, Yahya S.;Elfaki, Imadeldin;Habib, Salem A.;Alnour, Tarig M.;Darwish, Ahmed B.;Youssef, Magdy M.
    • Journal of Microbiology and Biotechnology
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    • v.32 no.5
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    • pp.551-563
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    • 2022
  • L-asparaginase (E.C. 3.5.1.1) purified from bacterial cells is widely used in the food industry, as well as in the treatment of childhood acute lymphoblastic leukemia. In the present study, the Burkholderia pseudomallei L-asparaginase gene was cloned into the pGEX-2T DNA plasmid, expressed in E. coli BL21 (DE3) pLysS, and purified to homogeneity using Glutathione Sepharose chromatography with 7.26 purification fold and 16.01% recovery. The purified enzyme exhibited a molecular weight of ~33.6 kDa with SDS-PAGE and showed maximal activity at 50℃ and pH 8.0. It retained 95.1, 89.6%, and 70.2% initial activity after 60 min at 30℃, 40℃, and 50℃, respectively. The enzyme reserved its activity at 30℃ and 37℃ up to 24 h. The enzyme had optimum pH of 8 and reserved 50% activity up to 24 h. The recombinant enzyme showed the highest substrate specificity towards L-asparaginase substrate, while no detectable specificity was observed for L-glutamine, urea, and acrylamide at 10 mM concentration. THP-1, a human leukemia cell line, displayed significant morphological alterations after being treated with recombinant L-asparaginase and the IC50 of the purified enzyme was recorded as 0.8 IU. Furthermore, the purified recombinant Lasparaginase improved cytotoxicity in liver cancer HepG2 and breast cancer MCF-7 cell lines, with IC50 values of 1.53 and 18 IU, respectively.

Inhibition of Aldehyde Dehydrogenase by the Active Oxygen Species (활성산소종에 의한 알데히드 탈수소 효소의 불활성화)

  • 문전옥;김태완;백기주;김기헌
    • YAKHAK HOEJI
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    • v.37 no.6
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    • pp.647-658
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    • 1993
  • The susceptibilities of aldehyde dehydrogenase (AldDH) and alcohol dehydrogenase (ADH) to active oxygen generated by xanthine-xanthine oxidase (XOD) system were studied. Incubation of AldDH with 2$\times$10$^{-3}$ units of XOD for 30 min at $25^{\circ}C$ resulted in the decrease of enzyme activity to 30% and it was inactivated completely when incubated with 5$\times$10$^{-3}$ units of XOD. Whereas 70% of ADH activity was retained after exposure to 5$\times$10$^{-3}$ units of XOD for 30 min, 40% of ADH activity was retained after exposure to 5$\times$10$^{-2}$ unit of XOD for 30 min. This inhibition effect by the active oxygen was preventable by catalase and glutathione, but not by SOD. The rates of the NADPH-dependent oxygen consumption by the liver S-9 mixture and microsomes were also determined in this study. Rate of oxygen consumption is increased in the liver S-9 mix and microsomes from phenobarbital-treated rat, and it was consistent with increased lipid peroxidation. In the presense of ethanol as a substrate, the oxygen consumption rates were increased. It is reported that hepatic AldDH activity is depressed in alcoholic liver diseases, however there is few report that explains the reason of depressed AldDH activity. These results are supportive of the theory that the increase in hepatic ethanol oxidation through the induced ME activity after chronic ethanol feeding generate oxygen radical at elevated rates and it leads to the depression of AldDH activity.

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Effect of Ethylacetate Fraction and Petroleum Ether Fraction of Ginseng on the Activities of Several Enzymes in Rabbit Liver. (인삼의 Ethylacetate 획분 및 Petroleum ether 획분이 토끼간의 몇 가지 효소활성에 미치는 영향)

  • 권윤의;정노팔
    • Journal of Ginseng Research
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    • v.8 no.1
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    • pp.15-21
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    • 1984
  • It has been known that ethyl acetate fraction and petroleum ether fraction prepared from ginseng are inhibitory to the L5178Y and sarcoma 180 cell at the concentrations o! 0.Imgfml or 0.2mg/ml. The shiny was carried out to examine effects of the two fractions on the activities of RNA polymerase, succinate dehydrogenase (SDH) and malate dehydrogenase (MDH) present in normal rabbit liver. The ethyl acetate fraction did not show any inhibitory effect on the RNA polymerase and SDH activity at the concentrations of 0.Imgfml and 0.2mglml, but inhibited malate dehydrogenase activity by 12.3% and 15.5%, at the same concentrations, respectively. The fraction also inhibited all the three enzymes at higher concentrations tested, but stimulated the succinate dehydrogenase activity at 0.024mg/ml to increase the enzyme activity by 14.6%. The petroleum ether fraction activated the SDH activity by 12.9% and 20.8%, at the concentration of 0.1mg/ml and 0.2mg/ml respectively. But the fraction did not affect the MDH activity at the same concentration. The fraction, however, inhibited the MDH activity and activated the SDH activity by 13.5% and 18.2%, at the concentration of 0.8mg/ml respectively.

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Phaleria macrocarpa Suppresses Oxidative Stress in Alloxan-induced Diabetic Rats by Enhancing Hepatic Antioxidant Enzyme Activity

  • Triastuti, Asih;Park, Hee-Juhn;Choi, Jong-Won
    • Natural Product Sciences
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    • v.15 no.1
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    • pp.37-43
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    • 2009
  • Oxidative stress is caused by an imbalance between the production of reactive oxygen and an ability of a biological system, to readily detoxify the reactive intermediates or easily repair the resulting damage. It has been suggested that developmental alloxan-induced liver damage is mediated through increases in oxidative stress. The anti-diabetic effect and antioxidant activity of Phaleria macrocarpa (PM) fractions were investigated in alloxan-induced diabetic rats. After two weeks administration of PM, the liver antioxidant enzyme and hyperglycemic state were evaluated. The results showed that oral administration of PM treatments reduced blood glucose levels in diabetic rats by oral administration (P < 0.05). Serum glutamic-oxaloacetic transaminase (sGOT) and serum glutamic-pyruvate-transaminase (sGPT) were also diminished by PM supplementation. The superoxide dismutase (SOD), catalase (CAT) and glutathione-peroxidase (GPx) activities, and glutathione (GSH) level in the alloxan-induced diabetic rats were significantly decreased (P < 0.05) compared to those in the normal rats but were restored by PM treatments. PM fractions also repressed the level of malondialdehyde (MDA) in the liver. Glutathione reductase (GR), glutathione-S-transferase (GST) and $\gamma$-glutamylcysteine synthase (GCS) were also reduced in alloxan-induced diabetic rats. PM fractions could restore the GR and GST activities, but the GCS activity was not affected in rat livers. From the results of the present study, the diabetic effect of the butanol fraction of PM against alloxan-induced diabetic rats was concluded to be mediated either by preventing the decline of hepatic antioxidant status or due to its indirect radical scavenging capacity.

Evaluation of Coffee Ground as a Feedstuff in Practical Diets for Olive Flounder Paralichthys olivaceus

  • Rahimnejad, Samad;Choi, Jin;Lee, Sang-Min
    • Fisheries and Aquatic Sciences
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    • v.18 no.3
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    • pp.257-264
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    • 2015
  • A 10-week feeding trial was carried out to investigate the feasibility of using spent coffee ground (CG) as a potential feed ingredient for olive flounder. Growth, feed utilization, body composition and antioxidant enzyme activity were examined. A control diet was formulated and three other diets were prepared to contain 5, 10 or 15% CG (designated as Con, CG5, CG10 and CG15, respectively) by replacing for wheat flour. Two hundred forty fish ($104{\pm}0.7g/fish$) were allotted to 12 circular tanks of 400 L capacity at a density of 20 fish per tank and fed the experimental diets twice daily. At the end of the feeding trial, fish fed the CG5 diet exhibited significantly (P < 0.05) higher growth performance than those fed the control diet. Also, fish fed the CG10 diet had a comparable growth to that of the control group, but further increase of dietary CG inclusion level to 15% resulted in significant decrease of growth performance. Fish fed the CG15 diet showed significantly lower feed efficiency and protein efficiency ratio than other treatments. Significantly lower muscle protein content was observed in fish fed CG15 diet compared to the control. Significant reduction in plasma cholesterol concentration was found in fish fed CG15 diet compared to control. No significant changes were found in alkyle and superoxide radicals scavenging activities of plasma, muscle and liver among dietary treatments. Also, liver total protein, total antioxidant capacity, catalase and glutathione peroxidase activities were not significantly influenced by dietary inclusion of CG. According to these results, we concluded that CG can be included up to 10% in the diet for olive flounder without any adverse effects on growth, feed utilization and antioxidant enzyme activity.

Cloning of Human Liver Cytosolic Sialidase from Genomic DNA Using Splicing by Overlap Extension and Its Characterization

  • HA KI-TAE;CHO SEUNG-HAK;KANG SUNG-KOO;KIM YEON-KYE;KIM JUNE-KI;KIM CHEORL-HO
    • Journal of Microbiology and Biotechnology
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    • v.15 no.4
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    • pp.722-727
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    • 2005
  • Cytosolic sialidase (Neu2), a member of the sialidase family that is responsible for hydrolysis of sialic acid from the terminal position of sialoglycoconjugates, is poorly expressed in skeletal muscle and not detected in any other adult tissues. Thus, we isolated Neu2 cDNA using splicing by overlap extension (SOEing). In order to further characterize this enzyme, a His-tagged derivative was expressed in the bacterial expression system and purified by $Ni^{2+}$-affinity chromatography. A recombinant product of approximately 42 kDa had sialidase activity toward 4-methyl-umbelliferyl-$\alpha$-D-N-acetylneuraminic acid (4MU-NeuAc). The optimal pH and temperature of the recombinant Neu2 for 4MU-NeuAc was 6.0 and $37.5^{\circ}C$, respectively. The metal ions, such as $Cu^{2+}\;and\;Cd^{2+}$, showed strong inhibitory effect on the activity of the enzyme. The enzyme efficiently hydrolyzed the gangliosides GM3 and GD3 and had relatively low activities on ganglioside GD1a and GD1b, $\alpha$2-3 sialyllactose, and sialylated glycoproteins such as fetuin, transferrin, and orsomucoid, but had hardly any activities on $\alpha$2-6 sialyllactose and ganglioside GM1 and GM2. We concluded that the recombinant Neu2 has a sialidase activity toward glycoproteins as well as gangliosides.

Alkaline Protease Hydrolysis of Chicken Liver for Food Utilization (Alkaline Protease에 의한 닭 간 단백질의 분해)

  • Lee, Keun-Taik;Park, Suk-Young;Kim, Woo-Jung
    • Korean Journal of Food Science and Technology
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    • v.23 no.1
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    • pp.25-30
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    • 1991
  • Chicken liver was enzymatically hydrolyzed with an alkaline protease and determined the optimal conditions of reaction temperature and time, pH and enzyme to substrate ratio(E/S ratio) for possible utilization as a protein supplementary ingredient. The functional properties of hydolysate measured were water and oil absorption capacity, emulsifying activity and viscosity and sensory properties were also evaluated. It was found that hydrolysis at $60^{\circ}C$ and pH 8.0 were most effective and the degree of hydrolysis increased with increasing E/S ratio. A decrease in water and oil absorption capacity and an increase in viscosity were found during hydrolysis. The lowest emulsifying activity and highest water absorption were measured for 1/2 hour-hydrolysate and little difference was found for those treated more than 1 hour. The sensory characteristics of odor showed no significant difference among the chicken liver hydrolysates while the brightness increased and red decreased significantly(p<0.01) as the hydrolysis proceeded.

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