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Volumn 8, Issue 2, 2013, Pages

In-Gel Determination of L-Amino Acid Oxidase Activity Based on the Visualization of Prussian Blue-Forming Reaction

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID OXIDASE; FERRIC FERROCYANIDE;

EID: 84873254155     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055548     Document Type: Article
Times cited : (16)

References (22)
  • 1
    • 84857261898 scopus 로고    scopus 로고
    • Advances in non-snake venom L-amino acid oxidase
    • Yu Z, Qiao H, (2012) Advances in non-snake venom L-amino acid oxidase. Appl Biochem Biotechnol 167: 1-13.
    • (2012) Appl Biochem Biotechnol , vol.167 , pp. 1-13
    • Yu, Z.1    Qiao, H.2
  • 2
    • 33645221476 scopus 로고    scopus 로고
    • The antimicrobial activity of Marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity
    • Lucas-Elio P, Gomez D, Solano F, Sanchez-Amat A, (2006) The antimicrobial activity of Marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity. J Bacteriol 188: 2493-2501.
    • (2006) J Bacteriol , vol.188 , pp. 2493-2501
    • Lucas-Elio, P.1    Gomez, D.2    Solano, F.3    Sanchez-Amat, A.4
  • 3
    • 0034792723 scopus 로고    scopus 로고
    • Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom
    • Sakurai Y, Takatsuka H, Yoshioka A, Matsui T, Suzuki M, et al. (2001) Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom. Toxicon 39(12):: 1827-33.
    • (2001) Toxicon , vol.39 , pp. 1827-1833
    • Sakurai, Y.1    Takatsuka, H.2    Yoshioka, A.3    Matsui, T.4    Suzuki, M.5
  • 4
    • 26844491279 scopus 로고    scopus 로고
    • Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californica
    • Yang H, Johnson PM, Ko KC, Kamio M, Germann MW, et al. (2005) Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californica. J Exp Biol 208: 3609-3622.
    • (2005) J Exp Biol , vol.208 , pp. 3609-3622
    • Yang, H.1    Johnson, P.M.2    Ko, K.C.3    Kamio, M.4    Germann, M.W.5
  • 5
    • 22144480320 scopus 로고    scopus 로고
    • Amino acid catabolism by an areA-regulated gene encoding an L-amino acid oxidase with broad substrate specificity in Aspergillus nidulans
    • Davis MA, Askin MC, Hynes MJ, (2005) Amino acid catabolism by an areA-regulated gene encoding an L-amino acid oxidase with broad substrate specificity in Aspergillus nidulans. Appl Environ Microbiol 71(7):: 3551-3555.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3551-3555
    • Davis, M.A.1    Askin, M.C.2    Hynes, M.J.3
  • 6
    • 46149107274 scopus 로고    scopus 로고
    • The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an L-amino acid oxidase
    • Gomez D, Espinosa E, Bertazzo M, Lucas-Elio P, Solano F, et al. (2008) The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an L-amino acid oxidase. Appl Microbiol Biotechnol 79(6):: 925-930.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 925-930
    • Gomez, D.1    Espinosa, E.2    Bertazzo, M.3    Lucas-Elio, P.4    Solano, F.5
  • 7
    • 79959801429 scopus 로고    scopus 로고
    • Correlation between pigmentation and larval settlement deterrence by Pseudoalteromonas sp. sf57
    • Huang YL, Li M, Yu Z, Qian PY, (2011) Correlation between pigmentation and larval settlement deterrence by Pseudoalteromonas sp. sf57. Biofouling 27(3):: 287-293.
    • (2011) Biofouling , vol.27 , pp. 287-293
    • Huang, Y.L.1    Li, M.2    Yu, Z.3    Qian, P.Y.4
  • 8
    • 0027272486 scopus 로고
    • Extensive accumulation of an extracellular L-amino-acid oxidase during gametogenesis of Chlumydomonas reinhardtii
    • Vallon O, Bulté L, Kuras R, Olive J, Wollman FA, (1993) Extensive accumulation of an extracellular L-amino-acid oxidase during gametogenesis of Chlumydomonas reinhardtii. Eur J Biochem 215: 351-360.
    • (1993) Eur J Biochem , vol.215 , pp. 351-360
    • Vallon, O.1    Bulté, L.2    Kuras, R.3    Olive, J.4    Wollman, F.A.5
  • 9
    • 0037145809 scopus 로고    scopus 로고
    • Antimicrobial action of achacin is mediated by L-amino acid oxidase activity
    • Ehara T, Kitajima S, Kanzawa N, Tamiya T, Tsuchiya T, (2002) Antimicrobial action of achacin is mediated by L-amino acid oxidase activity. FEBS Lett 531(3):: 509-512.
    • (2002) FEBS Lett , vol.531 , pp. 509-512
    • Ehara, T.1    Kitajima, S.2    Kanzawa, N.3    Tamiya, T.4    Tsuchiya, T.5
  • 10
    • 18544385783 scopus 로고    scopus 로고
    • Ammonia sensors and their applications-a review
    • Timmer B, Olthuis W, van den Berg A, (2005) Ammonia sensors and their applications-a review. Sensor Actuat B 107: 666-677.
    • (2005) Sensor Actuat B , vol.107 , pp. 666-677
    • Timmer, B.1    Olthuis, W.2    van den Berg, A.3
  • 11
    • 70349765719 scopus 로고    scopus 로고
    • Optimization of medium and cultivation conditions for L-amino acid oxidase production by Aspergillus fumigatus
    • Singh S, Gogoi BK, Bezbaruah RL, (2009) Optimization of medium and cultivation conditions for L-amino acid oxidase production by Aspergillus fumigatus. Can J Microbiol 55(9):: 1096-1102.
    • (2009) Can J Microbiol , vol.55 , pp. 1096-1102
    • Singh, S.1    Gogoi, B.K.2    Bezbaruah, R.L.3
  • 12
    • 84858428504 scopus 로고    scopus 로고
    • Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis Pitviper venom
    • Okubo BM, Silva ON, Migliolo L, Gomes DG, Porto WF, et al. (2012) Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis Pitviper venom. PLoS ONE 7(3):: e33639.
    • (2012) PLoS ONE , vol.7
    • Okubo, B.M.1    Silva, O.N.2    Migliolo, L.3    Gomes, D.G.4    Porto, W.F.5
  • 13
    • 33845925842 scopus 로고    scopus 로고
    • Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and 15 N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase
    • Ralph EC, Anderson MA, Cleland WW, Fitzpatrick PF, (2006) Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and 15 N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase. Biochemistry 45(51):: 15844-15852.
    • (2006) Biochemistry , vol.45 , pp. 15844-15852
    • Ralph, E.C.1    Anderson, M.A.2    Cleland, W.W.3    Fitzpatrick, P.F.4
  • 14
    • 0015072056 scopus 로고
    • Fluorescence Reaction for Amino Acids
    • Roth M, (1971) Fluorescence Reaction for Amino Acids. Anal Chem 43(7):: 880-882.
    • (1971) Anal Chem , vol.43 , pp. 880-882
    • Roth, M.1
  • 15
    • 79955101542 scopus 로고    scopus 로고
    • In-gel detection of L-amino acid oxidases based on the visulisation of hydrogen peroxide production
    • Rau JE, Fischer U, (2011) In-gel detection of L-amino acid oxidases based on the visulisation of hydrogen peroxide production. J Microbiol Methods 85(3):: 228-229.
    • (2011) J Microbiol Methods , vol.85 , pp. 228-229
    • Rau, J.E.1    Fischer, U.2
  • 16
    • 0034922653 scopus 로고    scopus 로고
    • Prussian blue and its analogues: electrochemistry and analytical applications
    • Karyakin AA, (2001) Prussian blue and its analogues: electrochemistry and analytical applications. Electroanalysis 13(10):: 813-819.
    • (2001) Electroanalysis , vol.13 , pp. 813-819
    • Karyakin, A.A.1
  • 17
    • 34548864382 scopus 로고    scopus 로고
    • A noval agar medium to detect hydrogen peroxide-producing bacteria based on the prussian blue-forming reaction
    • Saito M, Seki M, Lida K, Nakayama H, Yoshiada S, (2007) A noval agar medium to detect hydrogen peroxide-producing bacteria based on the prussian blue-forming reaction. Microbiol Immunol 51(9):: 889-892.
    • (2007) Microbiol Immunol , vol.51 , pp. 889-892
    • Saito, M.1    Seki, M.2    Lida, K.3    Nakayama, H.4    Yoshiada, S.5
  • 18
    • 77953617386 scopus 로고    scopus 로고
    • Involvement of an L-amino acid oxidase in the activity of the marine bacterium Pseudoalteromonas flavipulchra against methicillin-resistant Staphylococcus aureus
    • Chen WM, Lin CY, Chen CA, Wang JT, Sheu SY, (2010) Involvement of an L-amino acid oxidase in the activity of the marine bacterium Pseudoalteromonas flavipulchra against methicillin-resistant Staphylococcus aureus. Enzyme Microb Technol 47: 52-58.
    • (2010) Enzyme Microb Technol , vol.47 , pp. 52-58
    • Chen, W.M.1    Lin, C.Y.2    Chen, C.A.3    Wang, J.T.4    Sheu, S.Y.5
  • 19
    • 0037145809 scopus 로고    scopus 로고
    • Antimicrobial action of achacin is mediated by L-amino acid oxidase activity
    • Ehara T, Kitajima S, Kanzawa N, Tamiya T, Tsuchiya T, (2002) Antimicrobial action of achacin is mediated by L-amino acid oxidase activity. FEBS Lett 531: 509-512.
    • (2002) FEBS Lett , vol.531 , pp. 509-512
    • Ehara, T.1    Kitajima, S.2    Kanzawa, N.3    Tamiya, T.4    Tsuchiya, T.5
  • 20
    • 35648961283 scopus 로고    scopus 로고
    • Gene expression and distribution of antibacterial L-amino acid oxidase in the rockfish Sebastes schlegeli
    • Kitani Y, Mori T, Nagai H, Toyooka K, Ishizaki S, et al. (2007) Gene expression and distribution of antibacterial L-amino acid oxidase in the rockfish Sebastes schlegeli. Fish Shellfish Immunol 23(6):: 1178-1186.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 1178-1186
    • Kitani, Y.1    Mori, T.2    Nagai, H.3    Toyooka, K.4    Ishizaki, S.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0037146488 scopus 로고    scopus 로고
    • Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kang D, Gho YS, Suh M, Kang C, (2002) Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Bull Korean Chem Soc 23: 1511-1512.
    • (2002) Bull Korean Chem Soc , vol.23 , pp. 1511-1512
    • Kang, D.1    Gho, Y.S.2    Suh, M.3    Kang, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.