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Volumn 65, Issue 12, 2004, Pages 1839-1851

Identification of oxidised proteins in the matrix of rice leaf mitochondria by immunoprecipitation and two-dimensional liquid chromatography-tandem mass spectrometry

Author keywords

CCO, cytochrome c oxidase; DNP, dinitrophenylhydrazine; ESI, electrospray ionisation; IP, immunoprecipitation; MDH, malate dehydrogenase; MS, mass spectrometry; ROS, reactive oxygen species; SMP, submitochondrial particle; TOF, time of flight

Indexed keywords

2,4 DINITROPHENOL; CARBONYL DERIVATIVE; TRYPSIN;

EID: 3242776324     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2004.04.007     Document Type: Article
Times cited : (136)

References (39)
  • 1
    • 0035984635 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Down's syndrome
    • Arbuzova S., Hutchin T., Cuckle H. Mitochondrial dysfunction and Down's syndrome. BioEssays. 24:2002;681-684
    • (2002) BioEssays , vol.24 , pp. 681-684
    • Arbuzova, S.1    Hutchin, T.2    Cuckle, H.3
  • 2
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272:1997;20313-20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 4
    • 0036182712 scopus 로고    scopus 로고
    • Optic nerve degeneration and mitochondrial dysfunction: Genetic and acquired optic neuropathies
    • Carelli V., Ross-Cisneros F.N., Sadun A.A. Optic nerve degeneration and mitochondrial dysfunction: genetic and acquired optic neuropathies. Neurochem. Int. 40:2002;573-584
    • (2002) Neurochem. Int. , vol.40 , pp. 573-584
    • Carelli, V.1    Ross-Cisneros, F.N.2    Sadun, A.A.3
  • 5
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew O., Whelan J., Millar A.H. Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem. 278:2004;46869-46877
    • (2004) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 7
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S.L., Stocker R., Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324:1997;1-18
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.L.2    Stocker, R.3    Davies, M.J.4
  • 8
    • 0031791713 scopus 로고    scopus 로고
    • Identification of tryptophan oxidation products in bovine alpha-crystallin
    • Finley E.L., Dillon J., Crouch R.K., Schey K.L. Identification of tryptophan oxidation products in bovine alpha-crystallin. Protein Sci. 7:1998;2391-2397
    • (1998) Protein Sci. , vol.7 , pp. 2391-2397
    • Finley, E.L.1    Dillon, J.2    Crouch, R.K.3    Schey, K.L.4
  • 10
    • 0033932601 scopus 로고    scopus 로고
    • Oxygen processing in photosynthesis: Regulation and signalling
    • Foyer C.H., Noctor G. Oxygen processing in photosynthesis: regulation and signalling. New Phytol. 146:2000;359-388
    • (2000) New Phytol. , vol.146 , pp. 359-388
    • Foyer, C.H.1    Noctor, G.2
  • 11
    • 0042164949 scopus 로고    scopus 로고
    • Redox proteomics: Identification of oxidatively, modified proteins
    • Ghezzi P., Bonetto V. Redox proteomics: identification of oxidatively, modified proteins. Proteomics. 3:2003;1145-1153
    • (2003) Proteomics , vol.3 , pp. 1145-1153
    • Ghezzi, P.1    Bonetto, V.2
  • 14
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jimenez A., Hernandez J.A., delRio L.A., Sevilla F. Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol. 114:1997;275-284
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jimenez, A.1    Hernandez, J.A.2    Delrio, L.A.3    Sevilla, F.4
  • 15
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels - A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen J. Electroblotting of multiple gels - a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods. 10:1984;203-209
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0037373455 scopus 로고    scopus 로고
    • Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein
    • Marnett L.J., Riggins J.N., West J.D. Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein. J. Clin. Invest. 111:2003;583-593
    • (2003) J. Clin. Invest. , vol.111 , pp. 583-593
    • Marnett, L.J.1    Riggins, J.N.2    West, J.D.3
  • 19
    • 0036008577 scopus 로고    scopus 로고
    • Evidence of mitochondrial involvement in the transduction of signals required for the induction of genes associated with pathogen attack and senescence
    • Maxwell D.P., Nickels R., McIntosh L. Evidence of mitochondrial involvement in the transduction of signals required for the induction of genes associated with pathogen attack and senescence. Plant J. 29:2002;269-279
    • (2002) Plant J. , vol.29 , pp. 269-279
    • Maxwell, D.P.1    Nickels, R.2    McIntosh, L.3
  • 20
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller I.M. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52:2001;561-591
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 21
    • 3242749880 scopus 로고    scopus 로고
    • Protein oxidation in plant mitochondria as a stress indicator
    • (in press)
    • Møller, I.M., Kristensen, B.K., 2004. Protein oxidation in plant mitochondria as a stress indicator. Photochem. Photobiol. Sci. (in press)
    • (2004) Photochem. Photobiol. Sci.
    • Møller, I.M.1    Kristensen, B.K.2
  • 22
  • 23
    • 0020174796 scopus 로고
    • Purification of plant mitochondria by isopycnic centrifugation in density gradients of percoll
    • Neuburger M., Journet E.P., Bligny R., Carde J.P., Douce R. Purification of plant mitochondria by isopycnic centrifugation in density gradients of percoll. Arch. Biochem. Biophys. 217:1982;312-323
    • (1982) Arch. Biochem. Biophys. , vol.217 , pp. 312-323
    • Neuburger, M.1    Journet, E.P.2    Bligny, R.3    Carde, J.P.4    Douce, R.5
  • 24
    • 84989674612 scopus 로고
    • NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles
    • Rasmusson A.G., Møller I.M. NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles. Physiol. Plant. 83:1991;357-365
    • (1991) Physiol. Plant , vol.83 , pp. 357-365
    • Rasmusson, A.G.1    Møller, I.M.2
  • 26
    • 0035526593 scopus 로고    scopus 로고
    • Photooxidation of lens proteins with xanthurenic acid: A putative chromophore for cataractogenesis
    • Roberts J.E., Finley E.L., Patat S.A., Schey K.L. Photooxidation of lens proteins with xanthurenic acid: a putative chromophore for cataractogenesis. Photochem. Photobiol. 74:2001;740-744
    • (2001) Photochem. Photobiol. , vol.74 , pp. 740-744
    • Roberts, J.E.1    Finley, E.L.2    Patat, S.A.3    Schey, K.L.4
  • 28
    • 0042665855 scopus 로고    scopus 로고
    • Proteomic analysis of rat heart in ischemia and ischemia-reperfusion using fluorescence two-dimensional difference gel electrophoresis
    • Sakai J., Ishikawa H., Kojima S., Satoh H., Yamamoto S., Kanaoka M. Proteomic analysis of rat heart in ischemia and ischemia-reperfusion using fluorescence two-dimensional difference gel electrophoresis. Proteomics. 3:2003;1318-1324
    • (2003) Proteomics , vol.3 , pp. 1318-1324
    • Sakai, J.1    Ishikawa, H.2    Kojima, S.3    Satoh, H.4    Yamamoto, S.5    Kanaoka, M.6
  • 29
    • 0023472472 scopus 로고
    • Tricine sodium dodecyl-sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-kDa to 100-kDa
    • Schägger H., von Jagow G. Tricine sodium dodecyl-sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-kDa to 100-kDa. Anal. Biochem. 166:1987;368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 30
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal. Chem. 68:1996;850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 31
    • 84989741846 scopus 로고
    • The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane
    • Struglics A., Fredlund K.M., Rasmusson A.G., Møller I.M. The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane. Physiol. Plant. 88:1993;19-28
    • (1993) Physiol. Plant , vol.88 , pp. 19-28
    • Struglics, A.1    Fredlund, K.M.2    Rasmusson, A.G.3    Møller, I.M.4
  • 33
    • 0032189813 scopus 로고    scopus 로고
    • A double stain for total and oxidized proteins from two-dimensional fingerprints
    • Talent J.M., Kong Y.L., Gracy R.W. A double stain for total and oxidized proteins from two-dimensional fingerprints. Anal. Biochem. 263:1998;31-38
    • (1998) Anal. Biochem. , vol.263 , pp. 31-38
    • Talent, J.M.1    Kong, Y.L.2    Gracy, R.W.3
  • 34
    • 0037044794 scopus 로고    scopus 로고
    • Environmental stress causes oxidative damage to plant mitochondria leading to inhibition of glycine decarboxylase
    • Taylor N.L., Day D.A., Millar A.H. Environmental stress causes oxidative damage to plant mitochondria leading to inhibition of glycine decarboxylase. J. Biol. Chem. 277:2002;42663-42668
    • (2002) J. Biol. Chem. , vol.277 , pp. 42663-42668
    • Taylor, N.L.1    Day, D.A.2    Millar, A.H.3
  • 35
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins
    • Taylor S.W., Fahy E., Murray J., Capaldi R.A., Ghosh S.S. Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins. J. Biol. Chem. 278:2003;19587-19590
    • (2003) J. Biol. Chem. , vol.278 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4    Ghosh, S.S.5
  • 37
    • 0027980816 scopus 로고
    • 2 - Selective generation of 2-oxo-histidine at the histidine 118
    • 2 - selective generation of 2-oxo-histidine at the histidine 118. J. Biol. Chem. 269:1994;2405-2410
    • (1994) J. Biol. Chem. , vol.269 , pp. 2405-2410
    • Uchida, K.1    Kawakishi, S.2
  • 38
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19:2001;241-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 241-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 39
    • 0001944482 scopus 로고
    • The redox levels and subcellular distribution of pyridine nucleotides in illuminated barley leaf protoplasts studied by rapid fractionation
    • Wigge B., Krömer S., Gardeström P. The redox levels and subcellular distribution of pyridine nucleotides in illuminated barley leaf protoplasts studied by rapid fractionation. Physiol. Plant. 88:1993;10-18
    • (1993) Physiol. Plant , vol.88 , pp. 10-18
    • Wigge, B.1    Krömer, S.2    Gardeström, P.3


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