• Title/Summary/Keyword: enzyme activity change

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Effect of Sam Hwa San on Na-K-ATPase Activity in Microsomal Fraction of Rabbit Cerebral Cortex (삼화산(三和散)이 대뇌피질(大腦皮質) microsome분획(分劃)에서 Na-K-ATPase활성(活性)에 미치는 영향(影響))

  • Kim, Gil-Seop;Jeong, Ji-Cheon
    • The Journal of Korean Medicine
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    • v.16 no.1 s.29
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    • pp.281-294
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    • 1995
  • The effect of Sam Hwa San on the Na-K-ATPase activity was evaluated in microsomal fraction prepared from rabbit cerebral cortex to determine whether Sam Hwa San affects Na-K-ATPase activity of nervous system. Sam Hwa San markedly inhibited the Na-K-ATPase activity in a dose-dependent manner with an estimated $I_{50}$ of 0.12%. Optimal pH for the Na-K-ATPase activity was at 7.5 in the presence or absence of Sam Hwa San. The degree of inhibition by the drug more increased at acidic and alkalic pHs than neutral pH. Kinetic studies of substrate and cationic activation of the enzyme indicate classic noncompetitive inhibition fashion for ATP, Na and K, showing significant reduction in Vmax without a change in Km. Dithiothreitol, a sulfhydryl reducing reagent, partially protects the inhibition of Na-K-ATPase activity by Sam Hwa San. Combination of Sam Hwa San and ouabain showed higher inhibition than cumulative inhibition. These results suggest that Sam Hwa San inhibits Na-K-ATPase activity in central nervous system by reacting with, at least a part, sulfhydryl group and ouabain binding site of the enzyme protein, but with different binding site from those of ATP, Na and K.

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Effect of Pharbitidis Seed Extract on the Antioxidant Enzyme Activity in B16F10 Murine Melanoma Cells by Oxidative Stress (산화적 스트레스상태에서 B16F10 Murine Melanoma 세포의 항산화효소 활성에 대한 흑축추출물의 효과)

  • 김안근;차은정
    • YAKHAK HOEJI
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    • v.48 no.1
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    • pp.93-98
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    • 2004
  • The purpose of this study was to evaluate the effect of pharbitidis seed extract (PE) on antioxidant enzymes. The cytotoxicities of PE were measured by 3- (4,5-dimethlthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay; The change of superoxide dismutase (SOD), glutathione peroxidase (GPx), and catalase (CAT) activity assay were measured. The SOD activities by PE-treated groups were lower than control group's one. In the co-treated with hydrogen peroxide ($H_2O$$_2$) group, SOD activity was higher than $H_2O$$_2$ treated group's activity In the case of GPx, GPx activities were increased in both PE-treated and co-treated with $H_2O$$_2$ group. In the case of CAT $H_2O$$_2$ treated group's activityies were very increased. The CAT activities by PE-treated groups were lower than control group's one, but the activity of co-treated group with H $_2$O$_2$ was higher than that of control group's one. These results suggest that PE has antioxidant activity.

Ripening Characteristics and Antioxidant Enzyme Activity of Ilmi under Heat Stress Condition

  • Hwang, Woon-Ha;Jeong, Jae-Hyeok;Lee, Hyeon-Seok;Choi, In-Bae;Ahn, Seung-Hyeon;Jeong, Han-Young;Yoon, Jong-Tak;Choi, Kyung-Jin
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.63 no.2
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    • pp.112-119
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    • 2018
  • Heat stress during the ripening stage reduces the yield and quality of rice. Considering the adverse effects of global warming, it is necessary to breed heat stress tolerant rice cultivars and analyze their stress tolerance characteristics. We investigated the ripening characteristics and antioxidant enzyme activity of Ilmi under heat stress condition during the ripening stage. Ripening rate, 1000 brown grain weight, and rice quality of Ilmi were not significantly changed by heat stress during the ripening stage. Leaf chlorophyll, chlorophyll a/b ratio, and malondialdehyde (MDA) contents of Ilmi leaves were also less changed than those of Ilpum. These results strongly suggested that Ilmi has heat tolerance characteristics during the ripening stage. Analysis of antioxidant enzyme activity of Ilmi revealed that peroxidase (POX) activity was significantly higher than that of Ilpum, and showed a significant correlation with the change in chlorophyll a/b ratio and hydrogen peroxide content of flag leaves of Ilmi. These data suggest that the high POX enzyme activity of Ilmi could be considered one of its major heat tolerance characteristics.

Immobilization of Endo- and Exoinulinase on Vinylsulfone Activated Agarose (Vinylsulfone Activated Agarose 에 Endo- 및 Exoinulinase의 고정화)

  • 한상배;송근섭;정용섭;손희숙;우순자;엄태봉
    • Microbiology and Biotechnology Letters
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    • v.20 no.1
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    • pp.20-24
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    • 1992
  • In order to reuse inulinase effectively, a method for immobilizing both endo- and exoinulinase to vinylsulfone activated agarose via covalent bond was investigated. The immobilized enzyme preparation had, respectively, 400 U for exoinulinase activity and 80 U for endoinu- Iinase activity per gram gel. A thermal stability by immobilization had increased in the case of exoinulinase. Optimum pHs for two immobilized enzymes were 4.4 to 5.0. Synergistic effect which depends on mixed ratio of two immobilized enzymes was the best when the mixed ratio of endo/exo lay between 0.1 and 0.5, and its activity of the mixed enzyme increased 1.7 times as compared to that of each immobilized enzyme. Inulinase activities of both of the immobilized enzymes did not change during 20 times experimental runs in a batch reactor.

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Enzyme Activities in the Soil of Quercus mongolica Forests (신갈나무 산림토양에서의 효소활성도)

  • Song In-Geun;Yong-Keel Choi;Byung-Re Min
    • The Korean Journal of Ecology
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    • v.18 no.4
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    • pp.503-512
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    • 1995
  • The present paper describes partial results of the study on the activities of microbes in the soil of Quercus mongolica forest from July, 1994 to April, 1995. To determine the relationship between structure and function of soil microbial ecosystem, the author investigated the seasonal change of physical environmental factors, microbial population and soil enzyme activities. The changes of pH was not significant and the temperature of surface soil was 2℃ higher than lower soil through out the year. Moisture contents (%) of soil samples ranged from 7.64% to 42.11%. However, soils of site 3 at Mt. Komdan in which vegetation is successional have higher moisture content than the others. The bacterial population increased in summer, but continuously decreased in autumn and winter, and then reincreased again in spring. Bacterial population of surface soil was higher than those of 30 cm depth all the year round. Dehydrogenase activity (DHA) was about two-fold higher throughout in surface soil compared to those of lower soil. And the correlation coefficient between DHA and bacterial population size was 0,713, It was suggested that DHA could be used as a primary index of soil microbial population and activity in soil ecosystem.

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Change of Chitotriosidase activity in Gaucher Patients by Enzyme Replacement Therapy (Caucher 환자의 효소 대치요법에 따른 Chititriosidase 활성도 변화)

  • YOO, Han Wook;IM, Dae Seong;YANG, Song Hyun
    • Journal of The Korean Society of Inherited Metabolic disease
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    • v.6 no.1
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    • pp.58-62
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    • 2006
  • Gaucher disease is an inherited disorder due to a deficiency in the activity of glucocerebrosidase (EC. 3.2.1.45) by genetic mutation which resulted from missense, nonsense, frameshift, deletion in long arm 21 of chromosome 1 (1q21). Gaucher disease is classified into the main three types as type 1 (nonneuronopathic), type 2 (acute neuronopathic) and type 3 (subacute neuronopathic) according to the progressive phase of manifestations and nervous system involvement. Gaucher disease patients had been treated by using the method as splenectomy and bone marrow transplantation. But enzyme replacement therapy as a more effective treatment has been available since the early 1990's. In order to treat Gaucher disease efficiently by using ERT, it is necessary to chase the progress of the therapy. In this study, therefore, we tried to chase the progress of the ERT by using the measurement of chitotriosidase activity in Gaucher disease patients.

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Studies on the Change of Enzyme Activities during the Fermentation of Tobacco Leaves (엽연초(葉煙草) 발효중(醱酵中) 효소활성도(酵素活性度)의 변화(變化)에 관(關)한 연구(硏究))

  • Kim, H.S.;Chun, J.K.;Lee, S.R.;Bae, H.W.;Sung, H.S.
    • Applied Biological Chemistry
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    • v.8
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    • pp.75-80
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    • 1967
  • In order to investigate the change of enzyme activities during the fermentation of tobacco leaves, whole and cut leaves were treated for twenty days at $30^{\circ}C$ and $39^{\circ}C$ by the normal procedure and inoculation of yeast, respectively, and the activity of several enzymes was measured at proper intervals. 1) Alpha-amylase activity was steadily decreased with the progress of fermentation. 2) Invertase and catalase activities were steadily decreased until the mid of the period, and then increased again toward the end of the fermentation. The latter enzyme activity showed more marked change than the former. 3) Most of the polyphenol oxidase activity were decreased abruptly in the early stage of the fermentation, and thereafter leveled down slowly. 4) Peroxidase activity was detected throughout the fermentation but no remarkable change was observed. 5) Protease activtty was not detected through the fermentation period.

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Purification and Characterization of Internal Invertase in Rhodosporidum toruloides Mating Type a Cells

  • Jeong, Youn-Kee;Cho, Kyung-Soon;Lee, Tae-Ho;Ryu, Beung-Ho
    • Preventive Nutrition and Food Science
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    • v.2 no.3
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    • pp.250-254
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    • 1997
  • The internal invertase of Rhodosporidium toruloids mating type a cells was purified to a single band on SDS-PAGE from cell-free extract by acid precipitation, ion exchange chromatogaphy andgel filtration. The determined molecular weight of he purified enzyme was about 95,000 by gel filtration and 100,000 daltons on SDS-polyacryamide gel electrophoresis. This enzyme didn't show any activity change by several metal ions except 15.4% decrease by {TEX}$Mn^{2+}${/TEX} and was strongly inhibited by 2-mercaptoethanol and SDS. The invertase maintained its activity at high level until 70℃, but inactivated at 80℃ almost completely. The optimal temperature and pH of the enzyme were about 60℃ and pH 5.0, respectively. The stable pH range of invertase was narrow from pH 3.0 to 6.0. The Km value and isoelectric point of enzyme were 3.4×{TEX}$10^{3}${/TEX} M, pH 4.4, respectively.

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Effects of Protein and Fiber on Antioxidant Enzyme Activites of Brain in Ethanol-Treated Rats (에탄올을 투여한 흰쥐 노조직의 항산화효소계 활성에 미치는 단백질과 섬유소의 영향)

  • 이미경
    • Journal of Nutrition and Health
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    • v.33 no.6
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    • pp.613-618
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    • 2000
  • This study was to investigate the effect of dietary protein and fiber on the antioxidant enzyme activities of brain in acute or chronic ethanol-treated rats. Male Sprague-Dawley rats were fed on diets containing two levels of protein(7%, 20%) with two levels of fiber (5%, 10%) Rats were administered 40%(v/v) ethanol(5g/kg body weight)orally 90min before decaptiation in acute ethanol-treated groups and 25%(v/v) ethanol(5g/kg body weight) once a day for 5 weeks in chronic ethanol treated-groups. The rats were sacrificed after 5 weeks of feeding periods. Superoxide dismutase and gluthathione S-transferase activities were lower in chronic ethanol-treated groups than acute ethanol-treated groups whereas catalase and glutathuone peroxidase activities were significantly increased by chronic ethanol treatment. Low protein supplement accelerated to change of their activities however dietary fiber levels did not affect antioxidant enzyme activities. Chronic ethanol treatment and/or low protein supplement results in increasing the brain lipid peroxide content but in lowering glutathione level. (Korean J Nutrition 33(6) ; 613~618, 2000)

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Enhanced Production of L-Aspartate ${\beta}-Decarboxylase$ by Nitrogen Source in Pseudomonas dacunhae

  • Kim, Dong-Chung;Lee, Sung-Dong;In, Man-Jin
    • Journal of Applied Biological Chemistry
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    • v.49 no.3
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    • pp.106-109
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    • 2006
  • Improvement of L-asparate ${\beta}-decarboxylase$ production from Pseudomonas dacunhae ATCC 21192 was attempted by optimizing fermentation conditions. Optimum carbon and nitrogen sources for cell growth and enzyme production were determined. L-Glutamate (2%) was the most suitable carbon source, and D-glucose, D-glycerol and fumarate repressed enzyme production. Yeast extract (2%) was the most effective as nitrogen source. A slight change of pH to 6.5 from medium pH resulted in a meaningful increase in the production of enzyme. The production of the enzyme was highly improved by using 2% yeast extract and 2% L-glutamate in culture media. Maximum L-asparate ${\beta}-decarboxylase$ activity reached up to over 24 U/mL-broth by 15 h flask fermentation.