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Volumn 5, Issue , 2015, Pages 1-8

Direct electron transfer biosensor for hydrogen peroxide carrying nanocomplex composed of horseradish peroxidase and Au-nanoparticle - Characterization and application to bienzyme systems

Author keywords

Au nanoparticle; Direct electron transfer; Electrochemical biosensor; Glucose oxidase; Horseradish peroxidase; Urate oxidase

Indexed keywords

ARMORACIA RUSTICANA;

EID: 84934874728     PISSN: None     EISSN: 22141812     Source Type: Journal    
DOI: 10.1016/j.ancr.2015.05.001     Document Type: Article
Times cited : (27)

References (47)
  • 1
    • 17144364673 scopus 로고    scopus 로고
    • Nanomaterial-based electrochemical biosensors
    • Wang J. Nanomaterial-based electrochemical biosensors. Analyst 2005, 130:421.
    • (2005) Analyst , vol.130 , pp. 421
    • Wang, J.1
  • 2
    • 33644613273 scopus 로고    scopus 로고
    • Application of nanoparticles in electrochemical sensors and biosensors
    • Luo X., Morrin A., Killard A.J., Smyth M.R. Application of nanoparticles in electrochemical sensors and biosensors. Electroanalysis 2006, 18:319-326.
    • (2006) Electroanalysis , vol.18 , pp. 319-326
    • Luo, X.1    Morrin, A.2    Killard, A.J.3    Smyth, M.R.4
  • 3
    • 0034142018 scopus 로고    scopus 로고
    • Direct electrochemistry of horseradish peroxidase immobilized on a colloid/cysteamine-modified gold electrode
    • Xiao Y., Ju H.-X., Chen H.-Y. Direct electrochemistry of horseradish peroxidase immobilized on a colloid/cysteamine-modified gold electrode. Anal. Biochem. 2000, 278:22-28.
    • (2000) Anal. Biochem. , vol.278 , pp. 22-28
    • Xiao, Y.1    Ju, H.-X.2    Chen, H.-Y.3
  • 4
    • 0037459369 scopus 로고    scopus 로고
    • "Plugging into Enzymes": nanowiring of redox enzymes by a gold nanoparticle
    • Xiao Y., Patolsky F., Katz E., Hainfeld J.F., Willner I. "Plugging into Enzymes": nanowiring of redox enzymes by a gold nanoparticle. Science 2003, 299:1877-1881.
    • (2003) Science , vol.299 , pp. 1877-1881
    • Xiao, Y.1    Patolsky, F.2    Katz, E.3    Hainfeld, J.F.4    Willner, I.5
  • 5
    • 52449090218 scopus 로고    scopus 로고
    • Reagentless H2O2 biosensor with high electron transfer efficiency carrying nanocomplex of horseradish peroxidase and Au-nanoparticle
    • Okawa Y., Sakai Y., Shiba F. Reagentless H2O2 biosensor with high electron transfer efficiency carrying nanocomplex of horseradish peroxidase and Au-nanoparticle. Electrochemistry 2008, 76:522-524.
    • (2008) Electrochemistry , vol.76 , pp. 522-524
    • Okawa, Y.1    Sakai, Y.2    Shiba, F.3
  • 6
    • 60549110374 scopus 로고    scopus 로고
    • High performance bioanode based on direct electron transfer of fructose dehydrogenase at gold nanoparticle-modified electrodes
    • Murata K., Suzuki M., Kajiya K., Nakamura N., Ohno H. High performance bioanode based on direct electron transfer of fructose dehydrogenase at gold nanoparticle-modified electrodes. Electrochem. Commun. 2009, 11:668-671.
    • (2009) Electrochem. Commun. , vol.11 , pp. 668-671
    • Murata, K.1    Suzuki, M.2    Kajiya, K.3    Nakamura, N.4    Ohno, H.5
  • 7
    • 0024764103 scopus 로고
    • Enzyme monolayer- and bilayer-modified tin oxide electrodes for the determination of hydrogen peroxide and glucose
    • Tatsuma T., Okawa Y., Watanabe T. Enzyme monolayer- and bilayer-modified tin oxide electrodes for the determination of hydrogen peroxide and glucose. Anal. Chem. 1989, 61:2352-2355.
    • (1989) Anal. Chem. , vol.61 , pp. 2352-2355
    • Tatsuma, T.1    Okawa, Y.2    Watanabe, T.3
  • 8
    • 0036558189 scopus 로고    scopus 로고
    • A method to construct a third-generation horseradish peroxidase biosensor: self-assembling gold nanoparticles to three-dimensional sol-gel network
    • Jia J., Wang B., Wu A., Cheng G., Li Z., Dong S. A method to construct a third-generation horseradish peroxidase biosensor: self-assembling gold nanoparticles to three-dimensional sol-gel network. Anal. Chem. 2002, 74:2217-2223.
    • (2002) Anal. Chem. , vol.74 , pp. 2217-2223
    • Jia, J.1    Wang, B.2    Wu, A.3    Cheng, G.4    Li, Z.5    Dong, S.6
  • 9
    • 0036667919 scopus 로고    scopus 로고
    • Renewable reagentless hydrogen peroxide sensor based on direct electron transfer of horseradish peroxidase immobilized on colloidal gold-modified electrode
    • Liu S.-Q., Ju H.-X. Renewable reagentless hydrogen peroxide sensor based on direct electron transfer of horseradish peroxidase immobilized on colloidal gold-modified electrode. Anal. Biochem. 2002, 307:110-116.
    • (2002) Anal. Biochem. , vol.307 , pp. 110-116
    • Liu, S.-Q.1    Ju, H.-X.2
  • 10
    • 33750299566 scopus 로고    scopus 로고
    • Direct electrochemistry of horseradish peroxidase based on biocompatible carboxymethyl chitosan-gold nanoparticle nanocomposite
    • Xu Q., Mao C., Liu N.-N., Zhu J.-J., Sheng J. Direct electrochemistry of horseradish peroxidase based on biocompatible carboxymethyl chitosan-gold nanoparticle nanocomposite. Biosens. Bioelectron. 2006, 22:768-773.
    • (2006) Biosens. Bioelectron. , vol.22 , pp. 768-773
    • Xu, Q.1    Mao, C.2    Liu, N.-N.3    Zhu, J.-J.4    Sheng, J.5
  • 11
    • 77956911285 scopus 로고    scopus 로고
    • Reagentless biosensor for hydrogen peroxide based on self-assembled films of horseradish peroxidase/laponite/chitosan and the primary investigation on the inhibitory effect by sulfide
    • Shan D., Li Q.-B., Ding S.-N., Xu J.-Q., Cosnier S., Xue H.-G. Reagentless biosensor for hydrogen peroxide based on self-assembled films of horseradish peroxidase/laponite/chitosan and the primary investigation on the inhibitory effect by sulfide. Biosens. Bioelectron. 2010, 26:536-541.
    • (2010) Biosens. Bioelectron. , vol.26 , pp. 536-541
    • Shan, D.1    Li, Q.-B.2    Ding, S.-N.3    Xu, J.-Q.4    Cosnier, S.5    Xue, H.-G.6
  • 12
    • 80052356896 scopus 로고    scopus 로고
    • A novel electrochemical sensor surface for the detection of hydrogen peroxide using cyclic bisureas/gold nanoparticle composite
    • Mathew M., Sandhyarani N. A novel electrochemical sensor surface for the detection of hydrogen peroxide using cyclic bisureas/gold nanoparticle composite. Biosens. Bioelectron. 2011, 28:210-215.
    • (2011) Biosens. Bioelectron. , vol.28 , pp. 210-215
    • Mathew, M.1    Sandhyarani, N.2
  • 13
    • 79952817561 scopus 로고    scopus 로고
    • A novel hydrogen peroxide biosensor based on the immobilization of hemoglobin on three-dimensionally ordered macroporous (3DOM) gold-nanoparticle-doped titanium dioxide (GTD) film
    • Wei N., Xin X., Du J., Li J. A novel hydrogen peroxide biosensor based on the immobilization of hemoglobin on three-dimensionally ordered macroporous (3DOM) gold-nanoparticle-doped titanium dioxide (GTD) film. Biosens. Bioelectron. 2011, 26:3602-3607.
    • (2011) Biosens. Bioelectron. , vol.26 , pp. 3602-3607
    • Wei, N.1    Xin, X.2    Du, J.3    Li, J.4
  • 14
    • 84862798189 scopus 로고    scopus 로고
    • Gold-coated silica-fiber hybrid materials for application in a novel hydrogen peroxide biosensor
    • Shen J., Yang X., Zhu Y., Kang H., Cao H., Li C. Gold-coated silica-fiber hybrid materials for application in a novel hydrogen peroxide biosensor. Biosens. Bioelectron. 2012, 34:132-136.
    • (2012) Biosens. Bioelectron. , vol.34 , pp. 132-136
    • Shen, J.1    Yang, X.2    Zhu, Y.3    Kang, H.4    Cao, H.5    Li, C.6
  • 15
    • 33746096072 scopus 로고
    • A study of the nucleation and growth processes in the synthesis of colloidal gold
    • Turkevich J., Stevenson P.C., Hillier J. A study of the nucleation and growth processes in the synthesis of colloidal gold. Discuss. Faraday Soc. 1951, 11:55-75.
    • (1951) Discuss. Faraday Soc. , vol.11 , pp. 55-75
    • Turkevich, J.1    Stevenson, P.C.2    Hillier, J.3
  • 17
    • 0003051583 scopus 로고
    • Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions
    • Frens G. Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions. Nature 1973, 241:20-22.
    • (1973) Nature , vol.241 , pp. 20-22
    • Frens, G.1
  • 18
    • 0035249615 scopus 로고    scopus 로고
    • Plasmon resonance measurements of the adsorption and adsorption kinetics of a biopolymer onto gold nanocolloids
    • Eck D., Helm C.A., Wagner N.J., Vaynberg K.A. Plasmon resonance measurements of the adsorption and adsorption kinetics of a biopolymer onto gold nanocolloids. Langmuir 2001, 17:957-960.
    • (2001) Langmuir , vol.17 , pp. 957-960
    • Eck, D.1    Helm, C.A.2    Wagner, N.J.3    Vaynberg, K.A.4
  • 19
    • 0018488111 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase C
    • Welinder K.G. Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase C. Eur. J. Biochem. 1979, 96:483-502.
    • (1979) Eur. J. Biochem. , vol.96 , pp. 483-502
    • Welinder, K.G.1
  • 20
    • 0034663390 scopus 로고    scopus 로고
    • The influence of temperature on the characterization of water-soluble polymers using asymmetric flow field-flow-fractionation coupled to multiangle laser light scattering
    • Viebke C., Williams P.A. The influence of temperature on the characterization of water-soluble polymers using asymmetric flow field-flow-fractionation coupled to multiangle laser light scattering. Anal. Chem. 2000, 72:3896-3901.
    • (2000) Anal. Chem. , vol.72 , pp. 3896-3901
    • Viebke, C.1    Williams, P.A.2
  • 21
    • 0015186143 scopus 로고
    • Horseradish peroxidase in plasma studied by gel filtration
    • Vegge T., Winther F.Ø., Olsen B.R. Horseradish peroxidase in plasma studied by gel filtration. Histochemie 1971, 28:16-22.
    • (1971) Histochemie , vol.28 , pp. 16-22
    • Vegge, T.1    Winther, F.Ø.2    Olsen, B.R.3
  • 23
    • 0016378041 scopus 로고
    • Proton balance in conversions between five oxidation-reduction states of horseradish peroxidase
    • Yamada H., Yamazaki I. Proton balance in conversions between five oxidation-reduction states of horseradish peroxidase. Arch. Biochem. Biophys. 1974, 165:728-738.
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 728-738
    • Yamada, H.1    Yamazaki, I.2
  • 24
    • 0033083556 scopus 로고    scopus 로고
    • Tethered mediator biosensor. Mediated electron transfer between redox enzyme and electrode via ferrocene anchored to electrode surface with long poly(oxyethylene) chain
    • Okawa Y., Nagano M., Hirota S., Kobayashi H., Ohno T., Watanabe M. Tethered mediator biosensor. Mediated electron transfer between redox enzyme and electrode via ferrocene anchored to electrode surface with long poly(oxyethylene) chain. Biosens. Bioelectron. 1999, 14:229-235.
    • (1999) Biosens. Bioelectron. , vol.14 , pp. 229-235
    • Okawa, Y.1    Nagano, M.2    Hirota, S.3    Kobayashi, H.4    Ohno, T.5    Watanabe, M.6
  • 25
    • 58149364211 scopus 로고
    • Kinetic models of horseradish peroxidase action on a graphite electrode
    • Ruzgas T., Gorton L., Emnéus J., Marko-Varga G. Kinetic models of horseradish peroxidase action on a graphite electrode. J. Electroanal. Chem. 1995, 391:41-49.
    • (1995) J. Electroanal. Chem. , vol.391 , pp. 41-49
    • Ruzgas, T.1    Gorton, L.2    Emnéus, J.3    Marko-Varga, G.4
  • 26
    • 0025977574 scopus 로고
    • Oxidase/peroxidase bilayer-modified electrodes as sensors for lactate, pyruvate, cholesterol and uric acid
    • Tatsuma T., Watanabe T. Oxidase/peroxidase bilayer-modified electrodes as sensors for lactate, pyruvate, cholesterol and uric acid. Anal. Chim. Acta 1991, 242:85-89.
    • (1991) Anal. Chim. Acta , vol.242 , pp. 85-89
    • Tatsuma, T.1    Watanabe, T.2
  • 27
    • 78650875615 scopus 로고    scopus 로고
    • Amperometric hydrogen peroxide biosensor based on a modified gold electrode with silver nanowires
    • Song M.-J., Hwang S.W., Whang D. Amperometric hydrogen peroxide biosensor based on a modified gold electrode with silver nanowires. J. Appl. Electrochem. 2010, 40:2099-2105.
    • (2010) J. Appl. Electrochem. , vol.40 , pp. 2099-2105
    • Song, M.-J.1    Hwang, S.W.2    Whang, D.3
  • 28
    • 84864414251 scopus 로고    scopus 로고
    • A nonenzymatic hydrogen peroxide sensor based on silver nanowires and chitosan film
    • Gao X., Jin L., Wu Q., Chen Z., Lin X. A nonenzymatic hydrogen peroxide sensor based on silver nanowires and chitosan film. Electroanalysis 2012, 24:1771-1777.
    • (2012) Electroanalysis , vol.24 , pp. 1771-1777
    • Gao, X.1    Jin, L.2    Wu, Q.3    Chen, Z.4    Lin, X.5
  • 29
    • 70349859992 scopus 로고    scopus 로고
    • A novel nonenzymatic hydrogen peroxide sensor based on multi-wall carbon nanotube/silver nanoparticle nanohybrids modified gold electrode
    • Zhao W., Wang H., Qin X., Wang X., Zhao Z., Miao Z., et al. A novel nonenzymatic hydrogen peroxide sensor based on multi-wall carbon nanotube/silver nanoparticle nanohybrids modified gold electrode. Talanta 2009, 80:1029-1033.
    • (2009) Talanta , vol.80 , pp. 1029-1033
    • Zhao, W.1    Wang, H.2    Qin, X.3    Wang, X.4    Zhao, Z.5    Miao, Z.6
  • 30
    • 84899888965 scopus 로고    scopus 로고
    • Rapid electrodeposition of a gold-Prussian blue nanocomposite with ultrahigh electroactivity for dual-potential amperometric biosensing of uric acid
    • Wang W., Qin C., Xie Q., Qin X., Chao L., Huang Y., et al. Rapid electrodeposition of a gold-Prussian blue nanocomposite with ultrahigh electroactivity for dual-potential amperometric biosensing of uric acid. Analyst 2014, 139:2904-2911.
    • (2014) Analyst , vol.139 , pp. 2904-2911
    • Wang, W.1    Qin, C.2    Xie, Q.3    Qin, X.4    Chao, L.5    Huang, Y.6
  • 31
    • 18844431828 scopus 로고    scopus 로고
    • Silver nanoparticle assemblies supported on glassy-carbon electrodes for the electro-analytical detection of hydrogen peroxide
    • Welch C.M., Banks C.E., Simm A.O., Compton R.G. Silver nanoparticle assemblies supported on glassy-carbon electrodes for the electro-analytical detection of hydrogen peroxide. Anal. Bioanal. Chem. 2005, 382:12-21.
    • (2005) Anal. Bioanal. Chem. , vol.382 , pp. 12-21
    • Welch, C.M.1    Banks, C.E.2    Simm, A.O.3    Compton, R.G.4
  • 32
    • 66349085790 scopus 로고    scopus 로고
    • A new amperometric nanostructured sensor for the analytical determination of hydrogen peroxide
    • Guascito M.R., Filippo E., Malitesta C., Manno D., Serra A., Turco A. A new amperometric nanostructured sensor for the analytical determination of hydrogen peroxide. Biosens. Bioelectron. 2008, 24:1063-1069.
    • (2008) Biosens. Bioelectron. , vol.24 , pp. 1063-1069
    • Guascito, M.R.1    Filippo, E.2    Malitesta, C.3    Manno, D.4    Serra, A.5    Turco, A.6
  • 33
    • 33646004333 scopus 로고    scopus 로고
    • Hydrogen peroxide biosensor based on myoglobin/colloidal gold nanoparticles immobilized on glassy carbon electrode by a Nafion film
    • Yang W., Li Y., Bai Y., Sun C. Hydrogen peroxide biosensor based on myoglobin/colloidal gold nanoparticles immobilized on glassy carbon electrode by a Nafion film. Sens. Actuators B Chem. 2006, 115:42-48.
    • (2006) Sens. Actuators B Chem. , vol.115 , pp. 42-48
    • Yang, W.1    Li, Y.2    Bai, Y.3    Sun, C.4
  • 34
    • 60349097760 scopus 로고    scopus 로고
    • Hydrogen peroxide biosensor based on the direct electrochemistry of myoglobin immobilized on silver nanoparticles doped carbon nanotubes film
    • Liu C.-Y., Hu J.-M. Hydrogen peroxide biosensor based on the direct electrochemistry of myoglobin immobilized on silver nanoparticles doped carbon nanotubes film. Biosens. Bioelectron. 2009, 24:2149-2154.
    • (2009) Biosens. Bioelectron. , vol.24 , pp. 2149-2154
    • Liu, C.-Y.1    Hu, J.-M.2
  • 35
    • 77952743653 scopus 로고    scopus 로고
    • Hydrogen peroxide biosensor based on a myoglobin/hydrophilic room temperature ionic liquid film
    • Safavi A., Farjami F. Hydrogen peroxide biosensor based on a myoglobin/hydrophilic room temperature ionic liquid film. Anal. Biochem. 2010, 402:20-25.
    • (2010) Anal. Biochem. , vol.402 , pp. 20-25
    • Safavi, A.1    Farjami, F.2
  • 36
    • 54849406806 scopus 로고    scopus 로고
    • Direct electrochemistry of hemoglobin entrapped in composite electrodeposited chitosan-multiwall carbon nanotubes and nanogold particles membrane and its electrocatalytic application
    • Liu C., Hu J. Direct electrochemistry of hemoglobin entrapped in composite electrodeposited chitosan-multiwall carbon nanotubes and nanogold particles membrane and its electrocatalytic application. Electroanalysis 2008, 20:1067-1072.
    • (2008) Electroanalysis , vol.20 , pp. 1067-1072
    • Liu, C.1    Hu, J.2
  • 37
    • 1342306786 scopus 로고    scopus 로고
    • Immobilization of hemoglobin on zirconium dioxide nanoparticles for preparation of a novel hydrogen peroxide biosensor
    • Liu S., Dai Z., Chen H., Ju H. Immobilization of hemoglobin on zirconium dioxide nanoparticles for preparation of a novel hydrogen peroxide biosensor. Biosens. Bioelectron. 2004, 19:963-969.
    • (2004) Biosens. Bioelectron. , vol.19 , pp. 963-969
    • Liu, S.1    Dai, Z.2    Chen, H.3    Ju, H.4
  • 38
    • 0001233062 scopus 로고
    • Oxidation-reduction potentials of horseradish peroxidase
    • Harbury H.A. Oxidation-reduction potentials of horseradish peroxidase. J. Biol. Chem. 1957, 225:1009-1024.
    • (1957) J. Biol. Chem. , vol.225 , pp. 1009-1024
    • Harbury, H.A.1
  • 39
    • 0018273821 scopus 로고
    • Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme
    • Conroy C.W., Tyma P., Daum P.H., Erman J.E. Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme. Biochim. Biophys. Acta - Protein Struct. 1978, 537:62-69.
    • (1978) Biochim. Biophys. Acta - Protein Struct. , vol.537 , pp. 62-69
    • Conroy, C.W.1    Tyma, P.2    Daum, P.H.3    Erman, J.E.4
  • 40
    • 0027119818 scopus 로고
    • Model analysis of enzyme monolayer- and bilayer-modified electrodes: the transient response
    • Tatsuma T., Watanabe T., Okawa Y. Model analysis of enzyme monolayer- and bilayer-modified electrodes: the transient response. Anal. Chem. 1992, 64:630-635.
    • (1992) Anal. Chem. , vol.64 , pp. 630-635
    • Tatsuma, T.1    Watanabe, T.2    Okawa, Y.3
  • 41
    • 0027119851 scopus 로고
    • Model analysis of enzyme monolayer- and bilayer-modified electrodes: the steady-state response
    • Tatsuma T., Watanabe T. Model analysis of enzyme monolayer- and bilayer-modified electrodes: the steady-state response. Anal. Chem. 1992, 64:625-630.
    • (1992) Anal. Chem. , vol.64 , pp. 625-630
    • Tatsuma, T.1    Watanabe, T.2
  • 42
    • 0019634405 scopus 로고
    • Immobilized enzyme chemically modified electrode as an amperometric sensor
    • Ianniello R.M., Yacynych A.M. Immobilized enzyme chemically modified electrode as an amperometric sensor. Anal. Chem. 1981, 53:2090-2095.
    • (1981) Anal. Chem. , vol.53 , pp. 2090-2095
    • Ianniello, R.M.1    Yacynych, A.M.2
  • 43
    • 0001805813 scopus 로고
    • A chemically-modified enzyme membrane electrode as an amperometric glucose sensor
    • Yao T. A chemically-modified enzyme membrane electrode as an amperometric glucose sensor. Anal. Chim. Acta 1983, 148:27-33.
    • (1983) Anal. Chim. Acta , vol.148 , pp. 27-33
    • Yao, T.1
  • 44
    • 84996277295 scopus 로고
    • Glucose sensor carrying monomolecular layer covalently bound to tin(IV) oxide electrode
    • Okawa Y., Tsuzuki H., Yoshida S., Watanabe T. Glucose sensor carrying monomolecular layer covalently bound to tin(IV) oxide electrode. Anal. Sci. 1989, 5:507-512.
    • (1989) Anal. Sci. , vol.5 , pp. 507-512
    • Okawa, Y.1    Tsuzuki, H.2    Yoshida, S.3    Watanabe, T.4
  • 45
    • 0001447103 scopus 로고
    • Studies on uricase: I. Preparation, purification, and properties of a cuproprotein
    • Mahler H.R., Hübscher G., Baum H. Studies on uricase: I. Preparation, purification, and properties of a cuproprotein. J. Biol. Chem. 1955, 216:625-642.
    • (1955) J. Biol. Chem. , vol.216 , pp. 625-642
    • Mahler, H.R.1    Hübscher, G.2    Baum, H.3
  • 46
    • 0016119605 scopus 로고
    • Enzyme electrode sensing oxygen for uric acid in serum and urine
    • Nanjo M., Guilbault G.G. Enzyme electrode sensing oxygen for uric acid in serum and urine. Anal. Chem. 1974, 46:1769-1772.
    • (1974) Anal. Chem. , vol.46 , pp. 1769-1772
    • Nanjo, M.1    Guilbault, G.G.2
  • 47
    • 0030757239 scopus 로고    scopus 로고
    • Identification of the true product of the urate oxidase reaction
    • Kahn K., Serfozo P., Tipton P.A. Identification of the true product of the urate oxidase reaction. J. Am. Chem. Soc. 1997, 119:5435-5442.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5435-5442
    • Kahn, K.1    Serfozo, P.2    Tipton, P.A.3


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