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  1. Article ; Audio / Video: Implication of hydraulic properties of bioremediated diesel-contaminated soil

    Hyun, S / Ahn, M.Y / Zimmerman, A.R / Kim, M / Kim, J.G

    Chemosphere. 2008 Apr., v. 71, issue 9

    2008  

    Keywords soil water retention ; wettability ; soil pore system ; bioremediation ; diesel fuel ; soil pollution ; hydraulic conductivity ; hydrocarbons ; microorganisms
    Language English
    Dates of publication 2008-04
    Size p. 1646-1653.
    Document type Article ; Audio / Video
    ZDB-ID 120089-6
    ISSN 1879-1298 ; 0045-6535 ; 0366-7111
    ISSN (online) 1879-1298
    ISSN 0045-6535 ; 0366-7111
    DOI 10.1016/j.chemosphere.2008.01.026
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  2. Article ; Audio / Video: Influence of a soil enzyme on iron-cyanide complex speciation and mineral adsorption

    Zimmerman, A.R / Kang, D.H / Ahn, M.Y / Hyun, S / Banks, M.K

    Chemosphere. 2008 Jan., v. 70, issue 6

    2008  

    Keywords laccase ; Coriolus versicolor ; enzyme activity ; oxidation ; iron ; cyanides ; chemical speciation ; adsorption ; montmorillonite ; aluminum hydroxide ; bioremediation
    Language English
    Dates of publication 2008-01
    Size p. 1044-1051.
    Document type Article ; Audio / Video
    ZDB-ID 120089-6
    ISSN 1879-1298 ; 0045-6535 ; 0366-7111
    ISSN (online) 1879-1298
    ISSN 0045-6535 ; 0366-7111
    DOI 10.1016/j.chemosphere.2007.07.075
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  3. Article ; Online: Characterization of NODs and TLRs in innate immune response of human cementoblast cells.

    Ahn, M Y / Yoon, H-E / Park, J-H / Lee, J / Min, S-K / Ahn, S-G / Yoon, J-H

    Oral diseases

    2013  Volume 19, Issue 4, Page(s) 374–380

    Abstract: Objectives: Microbial Pattern-recognition receptors (PRRs), such as Toll-like receptors (TLRs) and the nucleotide-binding oligomerization domains (NODs), are essential for mammalian innate immune response. In this study, we examined the characterization ...

    Abstract Objectives: Microbial Pattern-recognition receptors (PRRs), such as Toll-like receptors (TLRs) and the nucleotide-binding oligomerization domains (NODs), are essential for mammalian innate immune response. In this study, we examined the characterization of NODs and TLRs on innate immune responses in human cementoblast (HCEM) cells.
    Materials and methods: The gene expression of NODs and TLRs was examined by RT-PCR. Interleukin-6 (IL-6) and Interleukin-8 (IL-8) productions in culture supernatants were measured by ELISA. Western blot analysis was performed to determine the degradation of IκB-α and Mitogen activated protein kinase (MAPK) activation in response to their agonist.
    Results: The levels of NODs and TLRs were apparently expressed in HCEM cells. Although a few gene levels were weak in intact cells, the stimulation by their agonists increased the gene expression of TLRs. NODs and TLRs led to the production of IL-6 or IL-8 and the degradation of IκB-α and MAPK activation in HCEM cells. Combination treatment of NOD1 or NOD2 agonists with TLRs agonists did not influence the production of IL-6 and IL-8 in HCEM cells.
    Conclusions: Our results indicate that NODs and TLRs are functionally expressed in HCEM cells and can trigger innate immune responses. However, NOD1 and NOD2 may not be cooperated with TLRs to elicit an immune response in HCEM cells.
    MeSH term(s) Cells, Cultured ; Dental Cementum/cytology ; Dental Cementum/immunology ; Dental Cementum/metabolism ; Enzyme Activation ; Gene Expression ; Humans ; Immunity, Innate/physiology ; Interleukin-6/biosynthesis ; Interleukin-6/genetics ; Interleukin-8/biosynthesis ; Interleukin-8/genetics ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/immunology ; Mitogen-Activated Protein Kinases/metabolism ; NF-kappa B/metabolism ; Receptors, Pattern Recognition/immunology ; Receptors, Pattern Recognition/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Toll-Like Receptors/genetics ; Toll-Like Receptors/immunology
    Chemical Substances Interleukin-6 ; Interleukin-8 ; Intracellular Signaling Peptides and Proteins ; NF-kappa B ; Receptors, Pattern Recognition ; Toll-Like Receptors ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
    Language English
    Publishing date 2013-05
    Publishing country Denmark
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1290529-x
    ISSN 1601-0825 ; 1354-523X
    ISSN (online) 1601-0825
    ISSN 1354-523X
    DOI 10.1111/odi.12012
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    Zs.A 4427: Show issues Location:
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  4. Article: Cytotoxicity and L-amino acid oxidase activity of animal venoms.

    Ahn, M Y / Lee, B M / Kim, Y S

    Archives of pharmacal research

    1997  Volume 20, Issue 1, Page(s) 13–16

    Abstract: The cytotoxicity of animal venoms (snakes, insects and marine animals) was measured against SNU-1 (stomach cancer cells) by dye uptake assay (MTT method). And also L-amino acid oxidase (AAO) activity of the venoms was compared. Among them, the venom ... ...

    Abstract The cytotoxicity of animal venoms (snakes, insects and marine animals) was measured against SNU-1 (stomach cancer cells) by dye uptake assay (MTT method). And also L-amino acid oxidase (AAO) activity of the venoms was compared. Among them, the venom fromOphiophagus hannah (king cobra) showed a strong AAO activity as well as a high potent cytotoxicity. Cytotoxic protein having a AAO was then partially purified by HPLC-GPC and two fractions (Fr. I and Fr. II) were collected. The IC(50) values of Fr. I and Fr. II were 0.19 mug/ml and 1.36 mug/ml, respectively. The results suggested that the cytotoxicity of king cobra venom may be due to its AAO activity.
    Language English
    Publishing date 1997-02
    Publishing country Korea (South)
    Document type Journal Article
    ZDB-ID 447623-2
    ISSN 1976-3786 ; 0253-6269
    ISSN (online) 1976-3786
    ISSN 0253-6269
    DOI 10.1007/BF02974035
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  5. Article: Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).

    Ahn, M Y / Lee, B M / Kim, Y S

    The international journal of biochemistry & cell biology

    1997  Volume 29, Issue 6, Page(s) 911–919

    Abstract: The aim of this project was to determine the cytotoxic components from the venom of king cobra, Ophiophagus hannah. Venom was purified by a combination of gel-filtration, ion-exchange and reversed-phase chromatographic steps. The biochemical properties ... ...

    Abstract The aim of this project was to determine the cytotoxic components from the venom of king cobra, Ophiophagus hannah. Venom was purified by a combination of gel-filtration, ion-exchange and reversed-phase chromatographic steps. The biochemical properties of the cytotoxic component were consistent with those of L-amino acid oxidase. The molecular weight of the enzyme was estimated to be 150,000 by gel filtration and 70,000 under the denaturing conditions of SDS-PAGE, indicating a dimer. It has an isoelectric point of 4.5 and is a glycoprotein. The N-terminal sequence of L-amino acid oxidase from the king cobra venom was determined to be SVINLEESFQEPEYE. The cytotoxicity of L-amino acid oxidase was observed in stomach cancer, murine melanoma, fibrosarcoma, colorectal cancer and Chinese hamster ovary cell lines. Cytotoxicity resulted in the loss of ability in attachment and inhibition of cell proliferation. The cytotoxic protein decreased the level of cell proliferation by 74% according to [3H]thymidine uptake assay. The mechanism of enzyme action may be related to the inhibition of thymidine incorporation and an interaction with DNA.
    MeSH term(s) Amino Acid Oxidoreductases/chemistry ; Amino Acid Oxidoreductases/isolation & purification ; Amino Acid Oxidoreductases/toxicity ; Amino Acid Sequence ; Amino Acids/analysis ; Animals ; CHO Cells ; Cell Survival/drug effects ; Cricetinae ; DNA-Binding Proteins/metabolism ; Elapid Venoms/enzymology ; Humans ; L-Amino Acid Oxidase ; Molecular Sequence Data ; Sequence Homology, Amino Acid ; Thymidine/metabolism ; Tumor Cells, Cultured
    Chemical Substances Amino Acids ; DNA-Binding Proteins ; Elapid Venoms ; Amino Acid Oxidoreductases (EC 1.4.-) ; L-Amino Acid Oxidase (EC 1.4.3.2) ; Thymidine (VC2W18DGKR)
    Language English
    Publishing date 1997-06
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1228429-4
    ISSN 1878-5875 ; 1357-2725
    ISSN (online) 1878-5875
    ISSN 1357-2725
    DOI 10.1016/s1357-2725(97)00024-1
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    Zs.A 431: Show issues Location:
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  6. Article: Purification and characterization of a plasmin-like protease from Tenodera sinensis (Chinese mantis).

    Hahn, B S / Cho, S Y / Ahn, M Y / Kim, Y S

    Insect biochemistry and molecular biology

    2001  Volume 31, Issue 6-7, Page(s) 573–581

    Abstract: A novel type of protease (mantis egg fibrinolytic enzyme, MEF-2) was isolated from the egg cases of Tenodera sinensis. The protease was homogeneous by SDS-PAGE and its apparent molecular mass was 32,900 Da. The amino acids in the N-terminal region were ... ...

    Abstract A novel type of protease (mantis egg fibrinolytic enzyme, MEF-2) was isolated from the egg cases of Tenodera sinensis. The protease was homogeneous by SDS-PAGE and its apparent molecular mass was 32,900 Da. The amino acids in the N-terminal region were Ile-Val-Gly-Gly-Glu-Glu-Ala-Val-Ala-Gly-Asp-Phe-Pro-Ile-Val-Ser-Leu-Gln-Glu. The enzyme was inhibited by PMSF, TLCK, aprotinin, benzamidine, soybean trypsin inhibitor and also slightly by elastatinal, EDTA, EGTA, cysteine and beta-mercaptoethanol, but TPCK, iodoacetate and E-64 did not affect the activity. MEF-2 was not sensitive to alpha(1)-antitrypsin but antithrombin III and alpha(2)-antiplasmin inhibited the enzyme. MEF-2 preferentially cleaved the oxidized B-chain of insulin between Arg(22) and Gly(23). Among chromogenic protease substrates, the most susceptible to MEF-2 hydrolysis was benzoyl-Phe-Val-Arg-p-nitroanilide with maximal activity at 30 degrees C and pH 5.0. These results indicate that MEF-2 belongs to the trypsin family. Upon incubation of crosslinked fibrin with MEF-2, a steady increase of D-dimer suggests that the enzyme has a strong fibrinolytic activity. In conclusion, MEF-2 is a new type of proteolytic enzyme and has some potential for practical application in fibrinolysis.
    MeSH term(s) Amino Acid Sequence ; Amino Acids ; Circular Dichroism ; Dimerization ; Fibrinolysin/antagonists & inhibitors ; Fibrinolysin/isolation & purification ; Fibrinolysin/metabolism ; Humans ; Mantodea/enzymology ; Molecular Sequence Data ; Plasminogen/metabolism ; Substrate Specificity
    Chemical Substances Amino Acids ; Plasminogen (9001-91-6) ; Fibrinolysin (EC 3.4.21.7)
    Language English
    Publishing date 2001-04-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483248-3
    ISSN 1879-0240 ; 0965-1748
    ISSN (online) 1879-0240
    ISSN 0965-1748
    DOI 10.1016/s0965-1748(00)00162-4
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  7. Article: Transformation of catechol in the presence of a laccase and birnessite

    Ahn, M.Y / Martinez, C.E / Archibald, D.D / Zimmerman, A.R / Bollag, J.M / Dec, J

    Soil biology & biochemistry. 2006 May, v. 38, issue 5

    2006  

    Abstract: The transformation of naturally occurring phenols to humic polymers through oxidative coupling reactions may involve oxidoreductive enzymes and soil minerals as catalysts. There is limited information on the possible inhibitory or synergistic ... ...

    Abstract The transformation of naturally occurring phenols to humic polymers through oxidative coupling reactions may involve oxidoreductive enzymes and soil minerals as catalysts. There is limited information on the possible inhibitory or synergistic interactions between oxidoreductases and mineral catalysts as they participate in oxidative coupling of phenolic substrates. In this study, a ternary system was investigated, in which a fungal enzyme (Trametes villosa laccase), birnessite (δ-MnO2), and a naturally occurring phenolic compound (catechol) were reacted together to model soil processes. Binary systems (catechol/laccase and catechol/birnessite) were included for comparison. In the absence of the mineral, T. villosa laccase (950 katal ml-1) transformed 31% of catechol, whereas birnessite (1 mg ml-1) in the absence of the enzyme showed a 24% catechol transformation. The percentages of catechol transformation in the binary systems did not accumulate in the ternary system; instead, birnessite and laccase tested together transformed only 36% of catechol. This suggested that birnessite had an inhibitory effect on substrate transformation by laccase catalysis. Enzyme assays indicated that inhibition was a result of enzyme deactivation by humic-like polymers produced by birnessite, and by Mn2+ ions released from the mineral. These observations underscore the importance of considering enzyme-soil mineral-organic matter interactions in studies of humus formation and contaminant removal.
    Keywords catechol ; birnessite ; biotransformation ; soil fungi ; soil enzymes ; enzyme activity ; enzyme activation ; reaction kinetics ; Trametes
    Language English
    Dates of publication 2006-05
    Size p. 1015-1020.
    Document type Article
    ZDB-ID 280810-9
    ISSN 0038-0717
    ISSN 0038-0717
    DOI 10.1016/j.soilbio.2005.08.016
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  8. Article: Cytotoxicity and L-amino acid oxidase activity of crude insect drugs.

    Ahn, M Y / Ryu, K S / Lee, Y W / Kim, Y S

    Archives of pharmacal research

    2000  Volume 23, Issue 5, Page(s) 477–481

    Abstract: The cytotoxicity of crude insect drugs was measured using HeLa cells originating from human cervix and uterine cancer, using the dye uptake assay in order to find potential anticancer agents. Three kinds of extracts (buffer, methanol and ethylacetate) ... ...

    Abstract The cytotoxicity of crude insect drugs was measured using HeLa cells originating from human cervix and uterine cancer, using the dye uptake assay in order to find potential anticancer agents. Three kinds of extracts (buffer, methanol and ethylacetate) were prepared from 26 insects and used as raw materials for the activity assay. Among these, the buffer extracts from Tabanus, Mylabris and Huechys showed a potent anticancer activity, and those from Catharsius, Red ant, Scorpion, Tabanus and Vespae Nidus showed a strong L-amino acid oxidase (AAO) activity as well as cytotoxicity. In contrast, buffer extracts from Gryllotalpa orientalis and Apriona germari larvae showed greater/more rapid Hela cell growth than that of other insects.
    MeSH term(s) Amino Acid Oxidoreductases/metabolism ; Animals ; Antineoplastic Agents/pharmacology ; HeLa Cells ; Humans ; Insecta ; L-Amino Acid Oxidase ; Venoms/pharmacology
    Chemical Substances Antineoplastic Agents ; Venoms ; Amino Acid Oxidoreductases (EC 1.4.-) ; L-Amino Acid Oxidase (EC 1.4.3.2)
    Language English
    Publishing date 2000-10-06
    Publishing country Korea (South)
    Document type Journal Article
    ZDB-ID 447623-2
    ISSN 1976-3786 ; 0253-6269
    ISSN (online) 1976-3786
    ISSN 0253-6269
    DOI 10.1007/bf02976576
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  9. Article: Purification and characterization of a plasmin-like protease from Tenodera sinensis (Chinese mantis)

    Hahn, B.S / Cho, S.Y / Ahn, M.Y / Kim, Y.S

    Insect biochemistry and molecular biology. Apr 27, 2001. v. 31 (6/7)

    2001  

    Abstract: A novel type of protease (mantis egg fibrinolytic enzyme, MEF-2) was isolated from the egg cases of Tenodera sinensis. The protease was homogeneous by SDS-PAGE and its apparent molecular mass was 32,900 Da. The amino acids in the N-terminal region were ... ...

    Abstract A novel type of protease (mantis egg fibrinolytic enzyme, MEF-2) was isolated from the egg cases of Tenodera sinensis. The protease was homogeneous by SDS-PAGE and its apparent molecular mass was 32,900 Da. The amino acids in the N-terminal region were Ile-Val-Gly-Gly-Glu-Glu-Ala-Val-Ala-Gly-Asp-Phe- Pro-Ile-Val-Ser-Leu-Gln-Glu. The enzyme was inhibited by PMSF, TLCK, aprotinin, benzamidine, soybean trypsin inhibitor and also slightly by elastatinal, EDTA, EGTA, cysteine and beta-mercaptoethanol, but TPCK, iodoacetate and E-64 did not affect the activity. MEF-2 was not sensitive to alpha1-antitrypsin but antithrombin III and alpha2-antiplasmin inhibited the enzyme. MEF-2 preferentially cleaved the oxidized B-chain of insulin between Arg22 and Gly23. Among chromogenic protease substrates, the most susceptible to MEF-2 hydrolysis was benzoyl-Phe-Val-Arg-p-nitroanilide with maximal activity at 30 degrees C and pH 5.0. These results indicate that MEF-2 belongs to the trypsin family. Upon incubation of crosslinked fibrin with MEF-2, a steady increase of D-dimer suggests that the enzyme has a strong fibrinolytic activity. In conclusion, MEF-2 is a new type of proteolytic enzyme and has some potential for practical application in fibrinolysis.
    Keywords Tenodera sinensis ; ova ; serine proteinases ; plasmin ; amino acids ; amino acid sequences ; enzyme activity ; enzyme inhibitors ; proteolysis ; fibrin ; fibrinolysis
    Language English
    Dates of publication 2001-0427
    Size p. 573-581.
    Document type Article
    ZDB-ID 1483248-3
    ISSN 1879-0240 ; 0965-1748
    ISSN (online) 1879-0240
    ISSN 0965-1748
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  10. Article: The effect of age on expression of endogenous plasminogen activators after focal cerebral ischemia in mice.

    Ahn, M Y / Zhang, Z G / Zhang, L / Chopp, M

    Brain research

    1999  Volume 833, Issue 1, Page(s) 112–116

    Abstract: We measured urokinase-type plasminogen activator (u-PA) and tissue-type plasminogen activator (t-PA) activity in the brain of 2-3 month old and 6-8 month old mice subjected to 4 h of middle cerebral artery (MCA) occlusion. t-PA activity was present in ... ...

    Abstract We measured urokinase-type plasminogen activator (u-PA) and tissue-type plasminogen activator (t-PA) activity in the brain of 2-3 month old and 6-8 month old mice subjected to 4 h of middle cerebral artery (MCA) occlusion. t-PA activity was present in all non-ischemic and ischemic young mouse brain. In contrast, t-PA activity was present in 46.7% of non-ischemic middle aged mouse brain and in 44.4% of ischemic middle aged mouse brain. u-PA activity was present in all young and middle aged non-ischemic brains.
    MeSH term(s) Aging/metabolism ; Animals ; Brain/metabolism ; Brain Ischemia/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Plasminogen Activators/metabolism ; Tissue Plasminogen Activator/metabolism ; Urokinase-Type Plasminogen Activator/metabolism
    Chemical Substances Plasminogen Activators (EC 3.4.21.-) ; Tissue Plasminogen Activator (EC 3.4.21.68) ; Urokinase-Type Plasminogen Activator (EC 3.4.21.73)
    Language English
    Publishing date 1999-06-26
    Publishing country Netherlands
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1200-2
    ISSN 1872-6240 ; 0006-8993
    ISSN (online) 1872-6240
    ISSN 0006-8993
    DOI 10.1016/s0006-8993(99)01430-4
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