메뉴 건너뛰기




Volumn 14, Issue 4, 2009, Pages 159-166

Protein carbonylation: Avoiding pitfalls in the 2,4-dinitrophenylhydrazine assay

Author keywords

Bacteria; Carbonyl assay; Nucleic acid; Oxidative stress; OxyBlot; Protein oxidation

Indexed keywords

2,4 DINITROPHENYLHYDRAZINE; BUFFER; CARBONYL DERIVATIVE; DEOXYRIBONUCLEASE; DNA; NUCLEIC ACID; OLIGONUCLEOTIDE; PROTEINASE K; RIBONUCLEASE; STREPTOMYCIN SULFATE; THIOL; 2,4-DINITROPHENYLHYDRAZINE; PHENYLHYDRAZINE DERIVATIVE; STREPTOMYCIN;

EID: 70350460031     PISSN: 13510002     EISSN: 17432928     Source Type: Journal    
DOI: 10.1179/135100009X392601     Document Type: Article
Times cited : (88)

References (23)
  • 1
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 1993; 62: 797-821.
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 2
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • Levine RL. Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic Biol Med 2002; 32: 790-796.
    • (2002) Free Radic Biol Med , vol.32 , pp. 790-796
    • Levine, R.L.1
  • 3
    • 0025102226 scopus 로고
    • Determination of carbonyl content in oxidatively modified proteins
    • Levine RL, Garland D, Oliver CN et al. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 1990; 186: 464-478.
    • (1990) Methods Enzymol , vol.186 , pp. 464-478
    • Levine, R.L.1    Garland, D.2    Oliver, C.N.3
  • 5
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification: Examination by Western blot immunoassay
    • Shacter E, Williams JA, Lim M, Levine RL. Differential susceptibility of plasma proteins to oxidative modification: examination by Western blot immunoassay. Free Radic Biol Med 1994; 17: 429-437.
    • (1994) Free Radic Biol Med , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 7
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo S, Levine RL. Methionine in proteins defends against oxidative stress. FASEB J 2009; 23: 464-472.
    • (2009) FASEB J , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 8
    • 39449105514 scopus 로고    scopus 로고
    • Protein carbonylation as a novel mechanism in redox signaling
    • Wong CM, Cheema AK, Zhang L, Suzuki YJ. Protein carbonylation as a novel mechanism in redox signaling. Circ Res 2008; 102: 310-318.
    • (2008) Circ Res , vol.102 , pp. 310-318
    • Wong, C.M.1    Cheema, A.K.2    Zhang, L.3    Suzuki, Y.J.4
  • 9
    • 34247375191 scopus 로고    scopus 로고
    • Protein oxidation implicated as the primary determinant of bacterial radioresistance
    • Daly MJ, Gaidamakova EK, Matrosova VY et al. Protein oxidation implicated as the primary determinant of bacterial radioresistance. PLoS Biol 2007; 5: e92.
    • (2007) PLoS Biol , vol.5
    • Daly, M.J.1    Gaidamakova, E.K.2    Matrosova, V.Y.3
  • 11
    • 3843151554 scopus 로고    scopus 로고
    • Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: Common targets and prevention by calorie restriction
    • Reverter-Branchat G, Cabiscol E, Tamarit J, Ros J. Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction. J Biol Chem 2004; 279: 31983-31989.
    • (2004) J Biol Chem , vol.279 , pp. 31983-31989
    • Reverter-Branchat, G.1    Cabiscol, E.2    Tamarit, J.3    Ros, J.4
  • 12
    • 58149498554 scopus 로고    scopus 로고
    • Oxidation of lipid and protein in horse mackerel (Trachurus trachurus) mince and washed minces during processing and storage
    • Eymard S, Baron C, Jacobsen C. Oxidation of lipid and protein in horse mackerel (Trachurus trachurus) mince and washed minces during processing and storage. Food Chem 2009; 114: 57-65.
    • (2009) Food Chem , vol.114 , pp. 57-65
    • Eymard, S.1    Baron, C.2    Jacobsen, C.3
  • 13
    • 34447554928 scopus 로고
    • A short course in bacterial genetics: A laboratory manual and handbook for Escherichia coli and related bacteria
    • NY: Cold Spring Harbor Laboratory Press
    • Miller JH. A short course in bacterial genetics: a laboratory manual and handbook for Escherichia coli and related bacteria. Plainview, NY: Cold Spring Harbor Laboratory Press, 1992.
    • (1992) Plainview
    • Miller, J.H.1
  • 14
    • 0025305991 scopus 로고
    • Metal-catalyzed oxidation of Escherichia coli glutamine synthetase: Correlation of structural and functional changes
    • Rivett AJ, Levine RL. Metal-catalyzed oxidation of Escherichia coli glutamine synthetase: correlation of structural and functional changes. Arch Biochem Biophys 1990; 278: 26-34.
    • (1990) Arch Biochem Biophys , vol.278 , pp. 26-34
    • Rivett, A.J.1    Levine, R.L.2
  • 16
    • 33644670810 scopus 로고    scopus 로고
    • Quantitation of protein on gels and blots by infrared fluorescence of Coomassie blue and Fast Green
    • Luo S, Wehr NB, Levine RL. Quantitation of protein on gels and blots by infrared fluorescence of Coomassie blue and Fast Green. Anal Biochem 2006; 350: 233-238.
    • (2006) Anal Biochem , vol.350 , pp. 233-238
    • Luo, S.1    Wehr, N.B.2    Levine, R.L.3
  • 18
    • 0000745994 scopus 로고
    • Isolierung und kristallisation des garungsferments enolase
    • Warburg O, Christian W. Isolierung und kristallisation des garungsferments enolase. Biochem Z 1942; 310: 384-421.
    • (1942) Biochem Z , vol.310 , pp. 384-421
    • Warburg, O.1    Christian, W.2
  • 19
    • 0035903569 scopus 로고    scopus 로고
    • Bacterial senescence: Protein oxidation in non-proliferating cells is dictated by the accuracy of the ribosomes
    • Ballesteros M, Fredriksson A, Henriksson J, Nystrom T. Bacterial senescence: protein oxidation in non-proliferating cells is dictated by the accuracy of the ribosomes. EMBO J 2001; 20: 5280-5289.
    • (2001) EMBO J , vol.20 , pp. 5280-5289
    • Ballesteros, M.1    Fredriksson, A.2    Henriksson, J.3    Nystrom, T.4
  • 20
    • 0024993131 scopus 로고
    • Protein that prevents mercaptan-mediated protein oxidation
    • Rhee SG, Kim K, Kim IH, Stadtman ER. Protein that prevents mercaptan-mediated protein oxidation. Methods Enzymol 1990; 186: 478-485.
    • (1990) Methods Enzymol , vol.186 , pp. 478-485
    • Rhee, S.G.1    Kim, K.2    Kim, I.H.3    Stadtman, E.R.4
  • 21
    • 0023766518 scopus 로고
    • Modulation of the hydrophobicity of glutamine synthetase by mixed-function oxidation
    • Cervera J, Levine RL. Modulation of the hydrophobicity of glutamine synthetase by mixed-function oxidation. FASEB J 1988; 2: 2591-2595.
    • (1988) FASEB J , vol.2 , pp. 2591-2595
    • Cervera, J.1    Levine, R.L.2
  • 22
    • 64449088672 scopus 로고    scopus 로고
    • Protein carbonylation: 2,4- dinitrophenylhydrazine reacts with both aldehydes/ketones and sulfenic acids
    • Dalle-Donne I, Carini M, Orioli M, et al. Protein carbonylation: 2,4- dinitrophenylhydrazine reacts with both aldehydes/ketones and sulfenic acids. Free Radic Biol Med 2009; 46: 1411-1419.
    • (2009) Free Radic Biol Med , vol.46 , pp. 1411-1419
    • Dalle-Donne, I.1    Carini, M.2    Orioli, M.3
  • 23
    • 0001664804 scopus 로고
    • Spectrophotometric studies of some 2,4-dinitrophenylhydrazones
    • Jones LA, Holmes JC, Seligman RB. Spectrophotometric studies of some 2,4-dinitrophenylhydrazones. Anal Chem 1956; 28: 191-198.
    • (1956) Anal Chem , vol.28 , pp. 191-198
    • Jones, L.A.1    Holmes, J.C.2    Seligman, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.