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Volumn 408, Issue 22, 2010, Pages 5399-5404

Potential enzyme toxicity of oxytetracycline to catalase

Author keywords

Catalase; Enzyme toxicity; Non covalent binding; Oxytetracycline; Spectroscopic techniques

Indexed keywords

ASSOCIATION CONSTANT; CATALASE; CIRCULAR DICHROISM; IN-VIVO; NEW STRATEGY; NONCOVALENT BINDING; NONRADIATIVE ENERGY TRANSFER; OXYTETRACYCLINE; PHYSIOLOGICAL PH; SECONDARY STRUCTURES; SPECTROSCOPIC TECHNIQUE; THERMODYNAMIC PARAMETER; TOXIC INTERACTIONS; TRYPTOPHAN RESIDUES; UV-VIS ABSORPTIONS; VAN DER WAALS; VETERINARY DRUG RESIDUE; VETERINARY DRUGS;

EID: 77956880315     PISSN: 00489697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.scitotenv.2010.08.005     Document Type: Article
Times cited : (54)

References (37)
  • 1
    • 33646581664 scopus 로고    scopus 로고
    • The fate and effect of oxytetracycline during the anaerobic digestion of manure from therapeutically treated calves
    • Arikan O.A., Sikora L.J., Mulbry W., Khan S.U., Rice C., Foster G.D. The fate and effect of oxytetracycline during the anaerobic digestion of manure from therapeutically treated calves. Process Biochem 2006, 41:1637-1643.
    • (2006) Process Biochem , vol.41 , pp. 1637-1643
    • Arikan, O.A.1    Sikora, L.J.2    Mulbry, W.3    Khan, S.U.4    Rice, C.5    Foster, G.D.6
  • 3
    • 0008192330 scopus 로고
    • Endotoxin pretreatment increases endogenous myocardial catalase activity and decreases ischemia-reperfusion injury of isolated rat hearts
    • Brown J.M., Grosso M.A., Terada L.S., Whitman G.J., Banerjee A., White C.W., et al. Endotoxin pretreatment increases endogenous myocardial catalase activity and decreases ischemia-reperfusion injury of isolated rat hearts. Proc Natl Acad Sci USA 1989, 86:2516-2520.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2516-2520
    • Brown, J.M.1    Grosso, M.A.2    Terada, L.S.3    Whitman, G.J.4    Banerjee, A.5    White, C.W.6
  • 4
    • 67349264084 scopus 로고    scopus 로고
    • Binding of brilliant red compound to lysozyme: insights into the enzyme toxicity of water-soluble aromatic chemicals
    • Chen F.F., Tang Y.N., Wang S.L., Gao H.W. Binding of brilliant red compound to lysozyme: insights into the enzyme toxicity of water-soluble aromatic chemicals. Amino Acids 2009, 36:399-407.
    • (2009) Amino Acids , vol.36 , pp. 399-407
    • Chen, F.F.1    Tang, Y.N.2    Wang, S.L.3    Gao, H.W.4
  • 5
    • 0346040439 scopus 로고    scopus 로고
    • Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy
    • Cui F.L., Fan J., Li J.P., Hu Z.D. Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy. Bioorg Med Chem 2004, 12:151-157.
    • (2004) Bioorg Med Chem , vol.12 , pp. 151-157
    • Cui, F.L.1    Fan, J.2    Li, J.P.3    Hu, Z.D.4
  • 6
    • 0002413436 scopus 로고
    • Delocalized excitation and excitation transfer
    • Academic Press, New York, O. Sinanoglu (Ed.)
    • Förster T. Delocalized excitation and excitation transfer. Modern Quantum Chemistry 1965, 3:93-137. Academic Press, New York. O. Sinanoglu (Ed.).
    • (1965) Modern Quantum Chemistry , vol.3 , pp. 93-137
    • Förster, T.1
  • 8
    • 33750053532 scopus 로고    scopus 로고
    • Impact of naringenin on oxytetracycline-mediated oxidative damage in kidney of rats
    • Gnanasoundari M., Pari L. Impact of naringenin on oxytetracycline-mediated oxidative damage in kidney of rats. Ren Fail 2006, 28:599-605.
    • (2006) Ren Fail , vol.28 , pp. 599-605
    • Gnanasoundari, M.1    Pari, L.2
  • 9
    • 0042549201 scopus 로고    scopus 로고
    • Toxicity of tetracyclines and tetracycline degradation products to environmentally relevant bacteria, including selected tetracycline-resistant bacteria
    • Halling-Sorensen B., Sengelov G., Tjornelund J. Toxicity of tetracyclines and tetracycline degradation products to environmentally relevant bacteria, including selected tetracycline-resistant bacteria. Arch Environ Contam Toxicol 2002, 42:263-271.
    • (2002) Arch Environ Contam Toxicol , vol.42 , pp. 263-271
    • Halling-Sorensen, B.1    Sengelov, G.2    Tjornelund, J.3
  • 10
    • 27644475219 scopus 로고    scopus 로고
    • Interaction of cromolyn sodium with human serum albumin: a fluorescence quenching study
    • Hu Y.J., Liu Y., Pi Z.B., Qu S.S. Interaction of cromolyn sodium with human serum albumin: a fluorescence quenching study. Bioorg Med Chem 2005, 13:6609-6614.
    • (2005) Bioorg Med Chem , vol.13 , pp. 6609-6614
    • Hu, Y.J.1    Liu, Y.2    Pi, Z.B.3    Qu, S.S.4
  • 11
    • 3242772209 scopus 로고    scopus 로고
    • Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
    • Huang B.X., Kim H.Y., Dass C. Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. J Am Soc Mass Spectrom 2004, 15:1237-1247.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 1237-1247
    • Huang, B.X.1    Kim, H.Y.2    Dass, C.3
  • 12
    • 33847337422 scopus 로고    scopus 로고
    • Uptake of oxytetracycline and its phytotoxicity to alfalfa (Medicago sativa L.)
    • Kong W.D., Zhu Y.G., Liang Y.C., Zhang J., Smith F.A., Yang M. Uptake of oxytetracycline and its phytotoxicity to alfalfa (Medicago sativa L.). Environ Pollut 2007, 147:187-193.
    • (2007) Environ Pollut , vol.147 , pp. 187-193
    • Kong, W.D.1    Zhu, Y.G.2    Liang, Y.C.3    Zhang, J.4    Smith, F.A.5    Yang, M.6
  • 13
    • 33845707338 scopus 로고    scopus 로고
    • Toxicological effects of three veterinary drugs and feed additives on fish
    • Li Z.L., Chen H.G., Xu Y., Kong Z.M. Toxicological effects of three veterinary drugs and feed additives on fish. J Ecol Rural Environ 2006, 22:84-86.
    • (2006) J Ecol Rural Environ , vol.22 , pp. 84-86
    • Li, Z.L.1    Chen, H.G.2    Xu, Y.3    Kong, Z.M.4
  • 14
    • 67349205424 scopus 로고    scopus 로고
    • Evaluation on the toxicity of nanoAg to bovine serum albumin
    • Liu R., Sun F., Zhang L., Zong W., Zhao X., Wang L., et al. Evaluation on the toxicity of nanoAg to bovine serum albumin. Sci Total Environ 2009, 407:4184-4188.
    • (2009) Sci Total Environ , vol.407 , pp. 4184-4188
    • Liu, R.1    Sun, F.2    Zhang, L.3    Zong, W.4    Zhao, X.5    Wang, L.6
  • 15
    • 0032042093 scopus 로고    scopus 로고
    • Influence of oxytetracycline and oxolinic acid on the immune response of rainbow trout (Oncorhynchus mykiss)
    • Lunden T., Miettinen S., Lonnstrom L.G., Lilius E.M., Bylund G. Influence of oxytetracycline and oxolinic acid on the immune response of rainbow trout (Oncorhynchus mykiss). Fish Shellfish Immunol 1998, 8:217-230.
    • (1998) Fish Shellfish Immunol , vol.8 , pp. 217-230
    • Lunden, T.1    Miettinen, S.2    Lonnstrom, L.G.3    Lilius, E.M.4    Bylund, G.5
  • 16
    • 33845681686 scopus 로고    scopus 로고
    • A simple method to measure effective catalase activities: optimization, validation, and application in green coffee
    • Montavon P., Kukic K.R., Bortlik K. A simple method to measure effective catalase activities: optimization, validation, and application in green coffee. Anal Biochem 2007, 360:207-215.
    • (2007) Anal Biochem , vol.360 , pp. 207-215
    • Montavon, P.1    Kukic, K.R.2    Bortlik, K.3
  • 17
    • 0036491512 scopus 로고    scopus 로고
    • Isolation of protein subpopulations undergoing protein-protein interactions
    • Nelson T.J., Backlund P.S., Yergey A.L., Alkon D.L. Isolation of protein subpopulations undergoing protein-protein interactions. Mol Cell Proteomics 2002, 1:253-259.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 253-259
    • Nelson, T.J.1    Backlund, P.S.2    Yergey, A.L.3    Alkon, D.L.4
  • 18
    • 33646258956 scopus 로고    scopus 로고
    • Influence of naringenin on oxytetracychne mediated oxidative damage in rat liver
    • Pari L., Gnanasoundari M. Influence of naringenin on oxytetracychne mediated oxidative damage in rat liver. Basic Clin Pharmacol Toxicol 2006, 98:456-461.
    • (2006) Basic Clin Pharmacol Toxicol , vol.98 , pp. 456-461
    • Pari, L.1    Gnanasoundari, M.2
  • 19
    • 33750976430 scopus 로고    scopus 로고
    • Structural insights into protein-uranyl interaction: towards an in silico detection method
    • Pible O., Guilbaud P., Pellequer J.L., Vidaud C., Quemeneur E. Structural insights into protein-uranyl interaction: towards an in silico detection method. Biochimie 2006, 88:1631-1638.
    • (2006) Biochimie , vol.88 , pp. 1631-1638
    • Pible, O.1    Guilbaud, P.2    Pellequer, J.L.3    Vidaud, C.4    Quemeneur, E.5
  • 21
    • 3242806075 scopus 로고    scopus 로고
    • Potential drug (oxytetracycline and oxolinic acid) pollution from Mediterranean sparid fish farms
    • Rigos G., Nengas I., Alexis M., Troisi G.M. Potential drug (oxytetracycline and oxolinic acid) pollution from Mediterranean sparid fish farms. Aquat Toxicol 2004, 69:281-288.
    • (2004) Aquat Toxicol , vol.69 , pp. 281-288
    • Rigos, G.1    Nengas, I.2    Alexis, M.3    Troisi, G.M.4
  • 22
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross P.D., Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 1981, 20:3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 23
    • 0018796397 scopus 로고
    • Fluorescence studies of native and modified neurophysins. Effects of peptides and pH
    • Shyamali S.S., Lillian D.R., Lawrence L., Esther B. Fluorescence studies of native and modified neurophysins. Effects of peptides and pH. Biochemistry 1979, 18:1026-1036.
    • (1979) Biochemistry , vol.18 , pp. 1026-1036
    • Shyamali, S.S.1    Lillian, D.R.2    Lawrence, L.3    Esther, B.4
  • 24
    • 33644980038 scopus 로고    scopus 로고
    • Binding analysis of glycyrrhetinic acid to human serum albumin: fluorescence spectroscopy, FTIR, and molecular modeling
    • Tang J., Luan F., Chen X. Binding analysis of glycyrrhetinic acid to human serum albumin: fluorescence spectroscopy, FTIR, and molecular modeling. Bioorg Med Chem 2006, 14:3210-3217.
    • (2006) Bioorg Med Chem , vol.14 , pp. 3210-3217
    • Tang, J.1    Luan, F.2    Chen, X.3
  • 25
    • 58949089579 scopus 로고    scopus 로고
    • Rapid detection of tetracyclines and their 4-epimer derivatives from poultry meat with bioluminescent biosensor bacteria
    • Virolainen N.E., Pikkemaat M.G., Elferink J.W.A., Karp M.T. Rapid detection of tetracyclines and their 4-epimer derivatives from poultry meat with bioluminescent biosensor bacteria. J Agric Food Chem 2008, 56:11065-11070.
    • (2008) J Agric Food Chem , vol.56 , pp. 11065-11070
    • Virolainen, N.E.1    Pikkemaat, M.G.2    Elferink, J.W.A.3    Karp, M.T.4
  • 26
    • 39749120538 scopus 로고    scopus 로고
    • Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin
    • Wang F., Huang W., Dai Z.X. Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin. J Mol Struct 2008, 875:509-514.
    • (2008) J Mol Struct , vol.875 , pp. 509-514
    • Wang, F.1    Huang, W.2    Dai, Z.X.3
  • 27
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process
    • Ware W.R. Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J Phys Chem 1962, 66:455-458.
    • (1962) J Phys Chem , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 28
    • 34447109949 scopus 로고    scopus 로고
    • Study on the interaction between salicylic acid and catalase by spectroscopic methods
    • Wu Y. Study on the interaction between salicylic acid and catalase by spectroscopic methods. J Pharm Biomed Anal 2007, 44:796-801.
    • (2007) J Pharm Biomed Anal , vol.44 , pp. 796-801
    • Wu, Y.1
  • 29
    • 34347352255 scopus 로고    scopus 로고
    • Binding of the environmental pollutant naphthol to bovine serum albumin
    • Wu T., Wu Q., Guan S., Su H., Cai Z. Binding of the environmental pollutant naphthol to bovine serum albumin. Biomacromolecules 2007, 8:1899-1906.
    • (2007) Biomacromolecules , vol.8 , pp. 1899-1906
    • Wu, T.1    Wu, Q.2    Guan, S.3    Su, H.4    Cai, Z.5
  • 31
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang J.T., Wu C.S., Martinez H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol 1986, 130:208-269.
    • (1986) Methods Enzymol , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 32
    • 67651230412 scopus 로고    scopus 로고
    • Probing the interaction of magnetic iron oxide nanoparticles with bovine serum albumin by spectroscopic techniques
    • Yang Q., Liang J., Han H. Probing the interaction of magnetic iron oxide nanoparticles with bovine serum albumin by spectroscopic techniques. J Phys Chem B 2009, 113:10454-10458.
    • (2009) J Phys Chem B , vol.113 , pp. 10454-10458
    • Yang, Q.1    Liang, J.2    Han, H.3
  • 33
    • 0032478116 scopus 로고    scopus 로고
    • Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding
    • Yuan T., Weljie A.M., Vogel H.J. Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding. Biochemistry 1998, 37:3187-3195.
    • (1998) Biochemistry , vol.37 , pp. 3187-3195
    • Yuan, T.1    Weljie, A.M.2    Vogel, H.J.3
  • 34
    • 44349193874 scopus 로고    scopus 로고
    • Binding analysis of pazufloxacin mesilate to catalase using spectroscopic methods
    • Zhang X., Jin J. Binding analysis of pazufloxacin mesilate to catalase using spectroscopic methods. J Mol Struct 2008, 882:96-100.
    • (2008) J Mol Struct , vol.882 , pp. 96-100
    • Zhang, X.1    Jin, J.2
  • 35
    • 67650991855 scopus 로고    scopus 로고
    • New strategy for the evaluation of CdTe quantum dot toxicity targeted to bovine serum albumin
    • Zhao L., Liu R., Zhao X., Yang B., Gao C., Hao X., et al. New strategy for the evaluation of CdTe quantum dot toxicity targeted to bovine serum albumin. Sci Total Environ 2009, 407:5019-5023.
    • (2009) Sci Total Environ , vol.407 , pp. 5019-5023
    • Zhao, L.1    Liu, R.2    Zhao, X.3    Yang, B.4    Gao, C.5    Hao, X.6
  • 36
    • 34548497392 scopus 로고    scopus 로고
    • Probing the binding of flavonoids to catalase by molecular spectroscopy
    • Zhu J.F., Zhang X., Li D.J., Jin J. Probing the binding of flavonoids to catalase by molecular spectroscopy. J Mol Struct 2007, 843:38-44.
    • (2007) J Mol Struct , vol.843 , pp. 38-44
    • Zhu, J.F.1    Zhang, X.2    Li, D.J.3    Jin, J.4
  • 37
    • 0034519583 scopus 로고    scopus 로고
    • Metabolites of oxytetracycline, tetracycline, and chlortetracycline and their distribution in egg white, egg yolk, and hen plasma
    • Zurhelle G., Petz M., Mueller-Seitz E., Siewert E. Metabolites of oxytetracycline, tetracycline, and chlortetracycline and their distribution in egg white, egg yolk, and hen plasma. J Agric Food Chem 2000, 48:6392-6396.
    • (2000) J Agric Food Chem , vol.48 , pp. 6392-6396
    • Zurhelle, G.1    Petz, M.2    Mueller-Seitz, E.3    Siewert, E.4


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