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Volumn 12, Issue 12, 2013, Pages 5709-5722

Development and validation of MRM methods to quantify protein isoforms of polyphenol oxidase in loquat fruits

Author keywords

isoform; loquat fruits; multiple reaction monitoring; polyphenol oxidase; transitions

Indexed keywords

CATECHOL OXIDASE; ISOENZYME; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

EID: 84890065180     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr4006712     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • Lange, V.; Picotti, P.; Domon, B.; Acbersold, R. Selected reaction monitoring for quantitative proteomics: a tutorial Mol. Syst. Biol. 2008, 4, 222
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Acbersold, R.4
  • 2
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative Mass Spectrometric Multiple Reaction Monitoring Assays for Major Plasma Proteins
    • Anderson, L.; Hunter, C. L. Quantitative Mass Spectrometric Multiple Reaction Monitoring Assays for Major Plasma Proteins Mol. Cell. Proteomics 2006, 5, 583-588
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 583-588
    • Anderson, L.1    Hunter, C.L.2
  • 3
    • 84888312487 scopus 로고    scopus 로고
    • MRMaid: The SRM assay design tool for Arabidopsis and other species
    • Fun, J.; Mohareb, F.; Jones, A. M. E.; Bessant, C. MRMaid: the SRM assay design tool for Arabidopsis and other species Front. Plant Sci. 2012, 3, 164
    • (2012) Front. Plant Sci. , vol.3 , pp. 164
    • Fun, J.1    Mohareb, F.2    Jones, A.M.E.3    Bessant, C.4
  • 4
    • 79952112243 scopus 로고    scopus 로고
    • Basic design of MRM assays for peptide quantification
    • James, A.; Jorgensen, C. Basic design of MRM assays for peptide quantification Methods Mol. Biol. 2010, 658, 167-185
    • (2010) Methods Mol. Biol. , vol.658 , pp. 167-185
    • James, A.1    Jorgensen, C.2
  • 6
    • 67650361220 scopus 로고    scopus 로고
    • Multiple products monitoring as a robust approach for peptide quantification
    • Baek, J. H.; Kim, H.; Shin, B.; Yu, M. H. Multiple products monitoring as a robust approach for peptide quantification J. Proteome Res. 2009, 8, 3625-3632
    • (2009) J. Proteome Res. , vol.8 , pp. 3625-3632
    • Baek, J.H.1    Kim, H.2    Shin, B.3    Yu, M.H.4
  • 8
    • 33745621292 scopus 로고    scopus 로고
    • Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: Determination of inhibitory phosphorylation status of cyclin-dependent kinases
    • Mayya, V.; Rezual, K.; Wu, L.; Fong, M. B.; Han, D. K. Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: determination of inhibitory phosphorylation status of cyclin-dependent kinases Mol. Cell. Proteomics 2006, 5, 1146-1157
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1146-1157
    • Mayya, V.1    Rezual, K.2    Wu, L.3    Fong, M.B.4    Han, D.K.5
  • 9
    • 0019741905 scopus 로고
    • Polyphenol oxidase and peroxidase in fruits and vegetables. CRC Crit
    • Vamos-Vigyazo, L. Polyphenol oxidase and peroxidase in fruits and vegetables. CRC Crit Rev. Food Sci. 1981, 15, 49-127
    • (1981) Rev. Food Sci. , vol.15 , pp. 49-127
    • Vamos-Vigyazo, L.1
  • 10
    • 0031900371 scopus 로고    scopus 로고
    • Diphenol oxidases, enzyme-cataysed browing and plant disease resistance
    • Walker, J. R. L.; Ferrar, P. H. Diphenol oxidases, enzyme-cataysed browing and plant disease resistance Biotechnol. Genet. Rev. 1998, 15, 457-498
    • (1998) Biotechnol. Genet. Rev. , vol.15 , pp. 457-498
    • Walker, J.R.L.1    Ferrar, P.H.2
  • 11
    • 49249153466 scopus 로고
    • Polyphenol oxidases in plants
    • Mayer, A. M.; Harel, E. Polyphenol oxidases in plants Phytochemistry 1979, 18, 193-215
    • (1979) Phytochemistry , vol.18 , pp. 193-215
    • Mayer, A.M.1    Harel, E.2
  • 12
    • 46149132278 scopus 로고
    • Polyphenol oxidases in plants-recent progress
    • Mayer, A. M. Polyphenol oxidases in plants-recent progress Phytochemistry 1987, 26, 11-20
    • (1987) Phytochemistry , vol.26 , pp. 11-20
    • Mayer, A.M.1
  • 13
    • 84987276731 scopus 로고
    • Phenolic composition and browning susceptibility of various apple cultivars at maturity
    • Amiot, M.; Tacchini, M.; Aubert, S.; Nicolas, J. Phenolic composition and browning susceptibility of various apple cultivars at maturity J. Food Sci. 1992, 57, 958-962
    • (1992) J. Food Sci. , vol.57 , pp. 958-962
    • Amiot, M.1    Tacchini, M.2    Aubert, S.3    Nicolas, J.4
  • 14
    • 0033786468 scopus 로고    scopus 로고
    • Honeys from different floral sources as inhibitors of enzymatic browning in fruit and vegetable homogenates
    • Chen, L.; Berenbaum, M.; Zangerl, A.; Engeseth, N. Honeys from different floral sources as inhibitors of enzymatic browning in fruit and vegetable homogenates J. Agric. Food Chem. 2000, 48, 4997-5000
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 4997-5000
    • Chen, L.1    Berenbaum, M.2    Zangerl, A.3    Engeseth, N.4
  • 15
    • 55249120036 scopus 로고    scopus 로고
    • Proteomics of multigenic families from species underrepresented in databases: The case of loquat (Eriobotrya japonica Lindl.) polyphenol oxidases
    • Sellés-Marchart, S.; Luque, I.; Casado-Vela, J.; Martínez-Esteso, M. J.; Bru-Martínez, R. Proteomics of multigenic families from species underrepresented in databases: the case of loquat (Eriobotrya japonica Lindl.) polyphenol oxidases J. Proteome Res. 2008, 7, 4095-4106
    • (2008) J. Proteome Res. , vol.7 , pp. 4095-4106
    • Sellés-Marchart, S.1    Luque, I.2    Casado-Vela, J.3    Martínez-Esteso, M.J.4    Bru-Martínez, R.5
  • 16
    • 0033103798 scopus 로고    scopus 로고
    • Immunological and molecular comparison of polyphenol oxidase in Rosaceae fruit trees
    • Haruta, M.; Murata, M.; Kadokura, H.; Homma, S. Immunological and molecular comparison of polyphenol oxidase in Rosaceae fruit trees Phytochemistry 1999, 50, 1021-1025
    • (1999) Phytochemistry , vol.50 , pp. 1021-1025
    • Haruta, M.1    Murata, M.2    Kadokura, H.3    Homma, S.4
  • 18
    • 7044238819 scopus 로고    scopus 로고
    • Polyphenol oxidase overexpression in transgenic Populus enhances resistance to herbivory by forest tent caterpillar (Malacosoma disstria)
    • Wang, J.; Constabel, C. P. Polyphenol oxidase overexpression in transgenic Populus enhances resistance to herbivory by forest tent caterpillar (Malacosoma disstria) Planta 2004, 220, 87-96
    • (2004) Planta , vol.220 , pp. 87-96
    • Wang, J.1    Constabel, C.P.2
  • 19
    • 0034800754 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of banana fruit polyphenol oxidase
    • Gooding, S. P.; Bird, C.; Robinson, P. S. Molecular cloning and characterisation of banana fruit polyphenol oxidase Planta 2001, 213, 748-757
    • (2001) Planta , vol.213 , pp. 748-757
    • Gooding, S.P.1    Bird, C.2    Robinson, P.S.3
  • 20
    • 0035661424 scopus 로고    scopus 로고
    • Two polyphenol oxidases are differentially expressed during vegetative and reproductive development and in response to wounding in the Fuji apple
    • Kim, J. Y.; Seo, Y. S.; Kim, J. E.; Sung, S. K.; Song, K. J.; An, G.; Kim, W. T. Two polyphenol oxidases are differentially expressed during vegetative and reproductive development and in response to wounding in the Fuji apple Plant Sci. 2001, 161, 1145-1152
    • (2001) Plant Sci. , vol.161 , pp. 1145-1152
    • Kim, J.Y.1    Seo, Y.S.2    Kim, J.E.3    Sung, S.K.4    Song, K.J.5    An, G.6    Kim, W.T.7
  • 21
    • 0029159295 scopus 로고
    • An apple polyphenol oxidase cDNA is up-regulated in wounded tissues
    • Boss, P. K.; Gardner, R. C.; Janssen, B. J.; Ross, G. S. An apple polyphenol oxidase cDNA is up-regulated in wounded tissues Plant Mol. Biol. 1995, 27, 429-433
    • (1995) Plant Mol. Biol. , vol.27 , pp. 429-433
    • Boss, P.K.1    Gardner, R.C.2    Janssen, B.J.3    Ross, G.S.4
  • 22
    • 84890024418 scopus 로고    scopus 로고
    • Ph.D. Thesis, Universidad de Alicante
    • Morante-Carriel, J. A. Ph.D. Thesis, Universidad de Alicante, 2012
    • (2012)
    • Morante-Carriel, J.A.1
  • 23
    • 32544455819 scopus 로고    scopus 로고
    • Isolation of a latent polyphenol oxidase from loquat fruit (Eriobotrya japonica Lindl.): Kinetic characterization and comparison with the active form
    • Sellés, S.; Casado-Vela, J.; Bru, R. Isolation of a latent polyphenol oxidase from loquat fruit (Eriobotrya japonica Lindl.): kinetic characterization and comparison with the active form Arch. Biochem. Biophys. 2006, 446, 175-185
    • (2006) Arch. Biochem. Biophys. , vol.446 , pp. 175-185
    • Sellés, S.1    Casado-Vela, J.2    Bru, R.3
  • 24
    • 0347134638 scopus 로고    scopus 로고
    • Protein extraction for two-dimensional electrophoresis from olive leaf, a plant tissue containing high levels of interfering compounds
    • Wang, W.; Scali, M.; Vignani, R.; Spadafora, A.; Sensi, E.; Mazzuca, S.; Cresti, M. Protein extraction for two-dimensional electrophoresis from olive leaf, a plant tissue containing high levels of interfering compounds Electrophoresis 2003, 24, 2369-2375
    • (2003) Electrophoresis , vol.24 , pp. 2369-2375
    • Wang, W.1    Scali, M.2    Vignani, R.3    Spadafora, A.4    Sensi, E.5    Mazzuca, S.6    Cresti, M.7
  • 25
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A.; Weinstein, D. Assay of proteins in the presence of interfering materials Anal. Biochem. 1976, 70, 241-250
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 26
    • 0028360749 scopus 로고
    • A protocol for protein estimation that gives a nearly constant color yield with simple proteins and nullifies the effects of four known interfering agents: Microestimation of peptide groups
    • Raghupathi, R. N.; Diwan, A. M. A protocol for protein estimation that gives a nearly constant color yield with simple proteins and nullifies the effects of four known interfering agents: microestimation of peptide groups Anal. Biochem. 1994, 219, 356-359
    • (1994) Anal. Biochem. , vol.219 , pp. 356-359
    • Raghupathi, R.N.1    Diwan, A.M.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
    • Laemmli, U. K. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Nature 1970, 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensivity using Coomasie Brilliant blue G-250 and R-250
    • Neuhoff, V.; Arold, N.; Taube, D.; Ehrhardt, W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensivity using Coomasie Brilliant blue G-250 and R-250 Electrophoresis 1988, 9, 255-262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 29
    • 84890013389 scopus 로고    scopus 로고
    • Improved tryptic digestion of proteins using 2,2,2-trifluoroethanol (TFE)
    • Santa Clara, CA
    • Meza, J. E.; Miller, C. A.; Fischer, S. M. Improved tryptic digestion of proteins using 2,2,2-trifluoroethanol (TFE). Agilent Technologies-Application Note 5989-1781EN; Agilent Technologies: Santa Clara, CA, 2004, (http://www.chem.agilent.com/Library/posters/Public/5989-1781EN.pdf).
    • (2004) Agilent Technologies-Application Note 5989-1781EN
    • Meza, J.E.1    Miller, C.A.2    Fischer, S.M.3
  • 30
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A.; Wilm, M.; Vorm, O.; Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal. Chem. 1996, 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 34
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A.; Rush, J.; Stemman, O.; Kirschner, M. W.; Gygi, S. P. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 6940-6945
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 35
    • 34548180275 scopus 로고    scopus 로고
    • A multiple reaction monitoring method for absolute quantification of the human liver alcohol dehydrogenase ADH1C1 isoenzyme
    • Janecki, D. J.; Bemis, K. G.; Tegeler, T. J.; Sanghani, P. C.; Zhai, L.; Hurley, T. D.; Bosron, W. F.; Wang, M. A multiple reaction monitoring method for absolute quantification of the human liver alcohol dehydrogenase ADH1C1 isoenzyme Anal. Biochem. 2007, 369, 18-26
    • (2007) Anal. Biochem. , vol.369 , pp. 18-26
    • Janecki, D.J.1    Bemis, K.G.2    Tegeler, T.J.3    Sanghani, P.C.4    Zhai, L.5    Hurley, T.D.6    Bosron, W.F.7    Wang, M.8
  • 36
    • 33751368850 scopus 로고    scopus 로고
    • Ion suppression: A major concern in mass spectrometry
    • Jessome, L. L.; Volmer, D. A. Ion suppression: a major concern in mass spectrometry LCGC North Am. 2006, 24, 498-510
    • (2006) LCGC North Am. , vol.24 , pp. 498-510
    • Jessome, L.L.1    Volmer, D.A.2
  • 37
    • 51249117296 scopus 로고    scopus 로고
    • If the antibody fails - A mass Western approach
    • Lehmann, U.; Wienkoop, S.; Tschoep, H.; Weckwerth, W. If the antibody fails-a mass Western approach Plant J. 2008, 55, 1039-1046
    • (2008) Plant J. , vol.55 , pp. 1039-1046
    • Lehmann, U.1    Wienkoop, S.2    Tschoep, H.3    Weckwerth, W.4
  • 38
    • 84863611387 scopus 로고    scopus 로고
    • GeLC-MRM Quantitation of Mutant KRAS Oncoprotein in Complex Biological Samples
    • Halvey, P. J.; Ferrone, C. R.; Liebler, D. C. GeLC-MRM Quantitation of Mutant KRAS Oncoprotein in Complex Biological Samples J. Proteome Res. 2012, 11, 3908-3913
    • (2012) J. Proteome Res. , vol.11 , pp. 3908-3913
    • Halvey, P.J.1    Ferrone, C.R.2    Liebler, D.C.3
  • 39
    • 0028486184 scopus 로고
    • Import, targeting, and processing of a plant polyphenol oxidase
    • Sommer, A.; Ne'eman, E.; Steffens, J. C.; Mayer, A. M.; Harel, E. Import, targeting, and processing of a plant polyphenol oxidase Plant Physiol. 1994, 105, 1301-1311
    • (1994) Plant Physiol. , vol.105 , pp. 1301-1311
    • Sommer, A.1    Ne'eman, E.2    Steffens, J.C.3    Mayer, A.M.4    Harel, E.5
  • 40
    • 0032538436 scopus 로고    scopus 로고
    • Purification and properties of a novel chloroplast stromal peptidase. Processing of polyphenol oxidase and other imported precursors
    • Koussevitzky, S.; Ne'eman, E.; Sommer, A.; Steffens, J.; Harel, E. Purification and properties of a novel chloroplast stromal peptidase. Processing of polyphenol oxidase and other imported precursors J. Biol. Chem. 1998, 273, 27064-27069
    • (1998) J. Biol. Chem. , vol.273 , pp. 27064-27069
    • Koussevitzky, S.1    Ne'eman, E.2    Sommer, A.3    Steffens, J.4    Harel, E.5
  • 41
    • 34547700094 scopus 로고    scopus 로고
    • Effect of detergents, trypsin and unsaturated fatty acids on latent loquat fruit polyphenol oxidase: Basis for the enzyme's activity regulation
    • Sellés, S.; Casado-Vela, J.; Bru, R. Effect of detergents, trypsin and unsaturated fatty acids on latent loquat fruit polyphenol oxidase: Basis for the enzyme's activity regulation Arch. Biochem. Biophys. 2007, 464, 295-305
    • (2007) Arch. Biochem. Biophys. , vol.464 , pp. 295-305
    • Sellés, S.1    Casado-Vela, J.2    Bru, R.3
  • 43
    • 84986737447 scopus 로고
    • Effects of limited proteolysis on broad bean polyphenol oxidase
    • King, R. S.; Flurkey, W. Effects of limited proteolysis on broad bean polyphenol oxidase J. Sci. Food Agric. 1987, 41, 231-240
    • (1987) J. Sci. Food Agric. , vol.41 , pp. 231-240
    • King, R.S.1    Flurkey, W.2
  • 45
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, Multiplexed Assays for Low Abundance Proteins in Plasma by Targeted Mass Spectrometry and Stable Isotope Dilution
    • Keshishian, H.; Addona, T.; Burgess, M.; Kuhn, E.; Carr, S. A. Quantitative, Multiplexed Assays for Low Abundance Proteins in Plasma by Targeted Mass Spectrometry and Stable Isotope Dilution Mol. Cell. Proteomics 2007, 6, 2212-2229
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4    Carr, S.A.5


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