메뉴 건너뛰기




Volumn 52, Issue 12, 2004, Pages 3967-3974

Identification of specific oxidatively modified proteins in chicken muscles using a combined immunologic and proteomic approach

Author keywords

3 nitrotyrosine; Carbonyls; Meat; Oxidative stress; Protein oxidation

Indexed keywords

3 NITROTYROSINE; ACTIN; ALPHA ENOLASE; ANTIOXIDANT; CARBONYL DERIVATIVE; CREATINE KINASE; ENOLASE; FREE RADICAL; HEAT SHOCK PROTEIN 70; MUSCLE PROTEIN; UNCLASSIFIED DRUG;

EID: 2942586687     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf035503d     Document Type: Article
Times cited : (59)

References (52)
  • 1
    • 0034079862 scopus 로고    scopus 로고
    • Free radicals and antioxidants in the year 2000. A historical look to the future
    • Gutteridge, J. M.; Halliwell, B. Free radicals and antioxidants in the year 2000. A historical look to the future. Ann. N. Y. Acad. Sci. 2000, 899, 136-147.
    • (2000) Ann. N. Y. Acad. Sci. , vol.899 , pp. 136-147
    • Gutteridge, J.M.1    Halliwell, B.2
  • 2
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean, R. T.; Fu, S.; Stocker, R.; Davies, M. J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 1997, 324 (Part 1), 1-18.
    • (1997) Biochem. J. , vol.324 , Issue.PART 1 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 3
    • 0034524859 scopus 로고    scopus 로고
    • Human studies related to protein oxidation: Protein carbonyl content as a marker of damage
    • Chevion, M.; Berenshtein, E.; Stadtman, E. R. Human studies related to protein oxidation: protein carbonyl content as a marker of damage. Free Radical Res. 2000, 33 (Suppl.), S99-108.
    • (2000) Free Radical Res. , vol.33 , Issue.SUPPL.
    • Chevion, M.1    Berenshtein, E.2    Stadtman, E.R.3
  • 4
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. The prototypic redox-based signaling mechanism
    • Stamler, J. S.; Lamas, S.; Fang, F. C. Nitrosylation. The prototypic redox-based signaling mechanism. Cell 2001, 106, 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 5
    • 0033429334 scopus 로고    scopus 로고
    • Stable markers of oxidant damage to proteins and their application in the study of human disease
    • Davies, M. J.; Fu, S.; Wang, H.; Dean, R. T. Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radical Biol. Med. 1999, 27, 1151-1163.
    • (1999) Free Radical Biol. Med. , vol.27 , pp. 1151-1163
    • Davies, M.J.1    Fu, S.2    Wang, H.3    Dean, R.T.4
  • 6
    • 0037096193 scopus 로고    scopus 로고
    • The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases
    • Giasson, B. I.; Ischiropoulos, H.; Lee, V. M.; Trojanowski, J. Q. The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases. Free Radical Biol. Med. 2002, 32, 1264-1275.
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 1264-1275
    • Giasson, B.I.1    Ischiropoulos, H.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 7
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal, M. F. Oxidatively modified proteins in aging and disease. Free Radical Biol. Med. 2002, 32, 797-803.
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 8
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in alzheimer's disease brain. Part I: Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna, A.; Aksenov, M.; Aksenova, M.; Thongboonkerd, V.; Klein, J. B.; Pierce, W. M.; Booze, R.; Markesbery, W. R.; Butterfield, D. A. Proteomic identification of oxidatively modified proteins in alzheimer's disease brain. part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radical Biol. Med. 2002, 33, 562-571.
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 9
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71
    • Castegna, A.; Aksenov, M.; Thongboonkerd, V.; Klein, J. B.; Pierce, W. M.; Booze, R.; Markesbery, W. R.; Butterfield, D. A. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71. J. Neurochem. 2002, 82, 1524-1532.
    • (2002) J. Neurochem. , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 10
    • 0037108986 scopus 로고    scopus 로고
    • Two-dimensional separation of the membrane protein sarcoplasmic reticulum Ca-ATPase for high-performance liquid chromatography-tandem mass spectrometry analysis of posttranslational protein modifications
    • Sharov, V. S.; Galeva, N. A.; Knyushko, T. V.; Bigelow, D. J.; Williams, T. D.; Schoneich, C. Two-dimensional separation of the membrane protein sarcoplasmic reticulum Ca-ATPase for high-performance liquid chromatography-tandem mass spectrometry analysis of posttranslational protein modifications. Anal. Biochem. 2002, 308, 328-335.
    • (2002) Anal. Biochem. , vol.308 , pp. 328-335
    • Sharov, V.S.1    Galeva, N.A.2    Knyushko, T.V.3    Bigelow, D.J.4    Williams, T.D.5    Schoneich, C.6
  • 11
    • 0242321030 scopus 로고    scopus 로고
    • Proteomic identification of age-dependent protein nitration in rat skeletal muscle
    • Kanski, J.; Alterman, M. A.; Schoneich, C. Proteomic identification of age-dependent protein nitration in rat skeletal muscle. Free Radical Biol. Med. 2003, 35, 1229-1239.
    • (2003) Free Radical Biol. Med. , vol.35 , pp. 1229-1239
    • Kanski, J.1    Alterman, M.A.2    Schoneich, C.3
  • 12
    • 0037218503 scopus 로고    scopus 로고
    • Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-evans Tokushima Fatty (OLETF) rat
    • Oh-Ishi, M.; Ueno, T.; Maeda, T. Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-evans Tokushima Fatty (OLETF) rat. Free Radical Biol. Med. 2003, 34, 11-22.
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 11-22
    • Oh-Ishi, M.1    Ueno, T.2    Maeda, T.3
  • 13
    • 84985275078 scopus 로고
    • Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation
    • Smith, D. M. Functional and biochemical changes in deboned turkey due to frozen storage and lipid oxidation. J. Food Sci. 1987, 52, 22-27.
    • (1987) J. Food Sci. , vol.52 , pp. 22-27
    • Smith, D.M.1
  • 14
    • 0000933366 scopus 로고    scopus 로고
    • Chemical, physical, and functional properties of cod proteins modified by a nonenzymatic free-radical-generating system
    • Srinivasan, S.; Hultin, H. O. Chemical, physical, and functional properties of cod proteins modified by a nonenzymatic free-radical-generating system. J. Agric. Food Chem. 1997, 45, 310-320.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 310-320
    • Srinivasan, S.1    Hultin, H.O.2
  • 15
    • 0001111625 scopus 로고    scopus 로고
    • Protein denaturation and functionality losses
    • Erikson, M. C., Hung, Y. C., Eds.; Chapman and Hall: New York; Chapter 8
    • Xiong, Y. L. Protein denaturation and functionality losses. In Quality in Frozen Foods; Erikson, M. C., Hung, Y. C., Eds.; Chapman and Hall: New York, 1997; Chapter 8, pp 111-140.
    • (1997) Quality in Frozen Foods , pp. 111-140
    • Xiong, Y.L.1
  • 16
    • 0000099948 scopus 로고    scopus 로고
    • Inhibition of protein and lipid oxidation in beef heart surimi-like material by antioxidants and combinations of pH, NaCl, and buffer type in the washing media
    • Srinivasan, S.; Xiong, Y. L.; Decker, E. A. Inhibition of protein and lipid oxidation in beef heart surimi-like material by antioxidants and combinations of pH, NaCl, and buffer type in the washing media. J. Agric. Food Chem. 1996, 44, 119-125.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 119-125
    • Srinivasan, S.1    Xiong, Y.L.2    Decker, E.A.3
  • 17
    • 2942603760 scopus 로고    scopus 로고
    • Thermal stability of oxidized muscle proteins as analyzed by differential scanning calorimetry
    • Institute of Food Technologists: Chicago, IL; Abstr. 38-35
    • Srinivasan, S.; Xiong, Y. L. Thermal stability of oxidized muscle proteins as analyzed by differential scanning calorimetry. In IFT Annual Meeting Book of Abstracts; Institute of Food Technologists: Chicago, IL, 1996; Abstr. 38-5.
    • (1996) IFT Annual Meeting Book of Abstracts
    • Srinivasan, S.1    Xiong, Y.L.2
  • 18
    • 0029854644 scopus 로고    scopus 로고
    • Storage stability of antioxidant-washed myofibrils from chicken white and red muscle
    • Liu, G.; Xiong, Y. L. Storage stability of antioxidant-washed myofibrils from chicken white and red muscle. J. Food Sci. 1996, 61, 890-894.
    • (1996) J. Food Sci. , vol.61 , pp. 890-894
    • Liu, G.1    Xiong, Y.L.2
  • 19
    • 0000915922 scopus 로고    scopus 로고
    • Chemical, physical and functional properties of oxidized turkey white muscle myofibrillar proteins
    • Decker, E. A.; Xiong, Y. L.; Calvert, J. T.; Crum, A. D.; Blanchard, S. P. Chemical, physical and functional properties of oxidized turkey white muscle myofibrillar proteins. J. Agric. Food Chem. 2003, 41, 186-189.
    • (2003) J. Agric. Food Chem. , vol.41 , pp. 186-189
    • Decker, E.A.1    Xiong, Y.L.2    Calvert, J.T.3    Crum, A.D.4    Blanchard, S.P.5
  • 20
    • 0031285814 scopus 로고    scopus 로고
    • Sulfhydryls in antioxidant-washed beef heart surimi
    • Srinivasan, S.; Xiong, Y. L. Sulfhydryls in antioxidant-washed beef heart surimi. J. Muscle Foods 1997, 8, 251-263.
    • (1997) J. Muscle Foods , vol.8 , pp. 251-263
    • Srinivasan, S.1    Xiong, Y.L.2
  • 21
    • 0034127455 scopus 로고    scopus 로고
    • Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin
    • Liu, G.; Xiong, Y. L. Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin. J. Agric. Food Chem. 2000, 48, 624-630.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 624-630
    • Liu, G.1    Xiong, Y.L.2
  • 22
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification: Examination by western blot immunoassay
    • Shacter, E.; Williams, J. A.; Lim, M.; Levine, R. L. Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay. Free Radical Biol. Med. 1994, 17, 429-437.
    • (1994) Free Radical Biol. Med. , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 23
    • 0029965252 scopus 로고    scopus 로고
    • Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis
    • Nakamura, A.; Goto, S. Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis. J. Biochem. (Tokyo) 1996, 119, 768-774.
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 768-774
    • Nakamura, A.1    Goto, S.2
  • 24
    • 0032539899 scopus 로고    scopus 로고
    • Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: Both modifications mimic effects of adenylylation
    • Berlett, B. S.; Levine, R. L.; Stadtman, E. R. Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: both modifications mimic effects of adenylylation. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 2784-2789.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2784-2789
    • Berlett, B.S.1    Levine, R.L.2    Stadtman, E.R.3
  • 26
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman, J. S.; Koppenol, W. H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am. J. Physiol. 1996, 271, C1424-C1437.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 28
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity
    • van der Vliet, A.; Eiserich, J. P.; Halliwell, B.; Cross, C. E. Formation of Reactive Nitrogen Species during Peroxidase-catalyzed Oxidation of Nitrite. A Potential Additional Mechanism of Nitric Oxide-Dependent Toxicity. J. Biol. Chem. 1997, 272, 7617-7625.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7617-7625
    • Van Der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 29
    • 0032529412 scopus 로고    scopus 로고
    • Myeloperoxidase and horseradish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide
    • Sampson, J. B.; Ye, Y.; Rosen, H.; Beckman, J. S. Myeloperoxidase and Horseradish Peroxidase Catalyze Tyrosine Nitration in Proteins from Nitrite and Hydrogen Peroxide. Arch. Biochem. Biophys. 1998, 356, 207-213.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 207-213
    • Sampson, J.B.1    Ye, Y.2    Rosen, H.3    Beckman, J.S.4
  • 30
    • 0029846920 scopus 로고    scopus 로고
    • Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase
    • Sampson, J. B.; Rosen, H.; Beckman, J. S. Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase. Methods Enzymol. 1996, 269, 210-218.
    • (1996) Methods Enzymol. , vol.269 , pp. 210-218
    • Sampson, J.B.1    Rosen, H.2    Beckman, J.S.3
  • 33
    • 0032715834 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good: A personal view of recent controversies
    • Halliwell, B.; Zhao, K.; Whiteman, M. Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good: a personal view of recent controversies. Free Radical Res. 1999, 31, 651-669.
    • (1999) Free Radical Res. , vol.31 , pp. 651-669
    • Halliwell, B.1    Zhao, K.2    Whiteman, M.3
  • 34
    • 0037189855 scopus 로고    scopus 로고
    • Chicken model for studying dietary antioxidants reveals that apple (Cox's Orange)/broccoli (Brassica oleracea L. var. italica) stabilizes erythrocytes and reduces oxidation of insoluble muscle proteins and lipids in cooked liver
    • Young, J. F.; Steffensen, C. L.; Nielsen, J. H.; Jensen, S. K.; Stagsted, J. Chicken model for studying dietary antioxidants reveals that apple (Cox's Orange)/broccoli (Brassica oleracea L. var. italica) stabilizes erythrocytes and reduces oxidation of insoluble muscle proteins and lipids in cooked liver. J. Agric. Food Chem. 2002, 50, 5058-5062.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 5058-5062
    • Young, J.F.1    Steffensen, C.L.2    Nielsen, J.H.3    Jensen, S.K.4    Stagsted, J.5
  • 35
    • 0034769635 scopus 로고    scopus 로고
    • Proteome analysis applied to meat science: Characterizing postmortem changes in porcine muscle
    • Lametsch, R.; Bendixen, E. Proteome analysis applied to meat science: characterizing postmortem changes in porcine muscle. J. Agric. Food Chem. 2001, 49, 4531-4537.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4531-4537
    • Lametsch, R.1    Bendixen, E.2
  • 36
    • 0023676995 scopus 로고
    • Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining
    • Hochstrasser, D. F.; Patchornik, A.; Merril, C. R. Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining. Anal. Biochem. 1988, 173, 412-423.
    • (1988) Anal. Biochem. , vol.173 , pp. 412-423
    • Hochstrasser, D.F.1    Patchornik, A.2    Merril, C.R.3
  • 38
    • 0032253972 scopus 로고    scopus 로고
    • Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: Strategies and applications
    • Jensen, O. N.; Larsen, M. R.; Roepstorff, P. Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: strategies and applications. Proteins 1998, Suppl 2, 74-89.
    • (1998) Proteins , Issue.SUPPL. 2 , pp. 74-89
    • Jensen, O.N.1    Larsen, M.R.2    Roepstorff, P.3
  • 39
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom, J.; Nordhoff, E.; Mirgorodskaya, E.; Ekman, R.; Roepstorff, P. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 1999, 34, 105-116.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 40
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
    • Cabiscol, E.; Piulats, E.; Echave, P.; Herrero, E.; Ros, J. Oxidative Stress Promotes Specific Protein Damage in Saccharomyces cerevisiae. J. Biol. Chem. 2000, 275, 27393-27398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 41
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in escherichia coli cells exposed to oxidative stress
    • Tamarit, J.; Cabiscol, E.; Ros, J. Identification of the Major Oxidatively Damaged Proteins in Escherichia coli Cells Exposed to Oxidative Stress. J. Biol. Chem. 1998, 273, 3027-3032.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 43
    • 0016695318 scopus 로고
    • Effects of specific chemical modification of actin
    • Chantler, P. D.; Gratzer, W. B. Effects of specific chemical modification of actin. Eur. J. Biochem. 1975, 60, 67-72.
    • (1975) Eur. J. Biochem. , vol.60 , pp. 67-72
    • Chantler, P.D.1    Gratzer, W.B.2
  • 44
    • 0037423394 scopus 로고    scopus 로고
    • Nitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine nitration induces defective cytoskeletal polymerization
    • Aslan, M.; Ryan, T. M.; Townes, T. M.; Coward, L.; Kirk, M. C.; Barnes, S.; Alexander, C. B.; Rosenfeld, S. S.; Freeman, B. A. Nitric Oxide-dependent Generation of Reactive Species in Sickle Cell Disease. Actin Tyrosine Nitration Induces Defective Cytoskeletal Polymerization. J. Biol. Chem. 2003, 278, 4194-4204.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4194-4204
    • Aslan, M.1    Ryan, T.M.2    Townes, T.M.3    Coward, L.4    Kirk, M.C.5    Barnes, S.6    Alexander, C.B.7    Rosenfeld, S.S.8    Freeman, B.A.9
  • 47
    • 0034024347 scopus 로고    scopus 로고
    • Oxidative modification of creatine kinase BB in Alzheimer's disease brain
    • Aksenov, M.; Aksenova, M.; Butterfield, D. A.; Markesbery, W. R. Oxidative modification of creatine kinase BB in Alzheimer's disease brain. J. Neurochem. 2000, 74, 2520-2527.
    • (2000) J. Neurochem. , vol.74 , pp. 2520-2527
    • Aksenov, M.1    Aksenova, M.2    Butterfield, D.A.3    Markesbery, W.R.4
  • 48
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid β-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • Allan-Butterfield, D.; Castegna, A.; Lauderback, C. M.; Drake, J. Evidence that amyloid β-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death. Neurobiol. Aging 2002, 23, 655.
    • (2002) Neurobiol. Aging , vol.23 , pp. 655
    • Allan-Butterfield, D.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 50
    • 0034853076 scopus 로고    scopus 로고
    • Peroxynitrite-induced oxidation of lipids: Implications for muscle foods
    • Brannan, R. G.; Decker, E. A. Peroxynitrite-induced oxidation of lipids: implications for muscle foods. J. Agric. Food Chem. 2001, 49, 3074-3079.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 3074-3079
    • Brannan, R.G.1    Decker, E.A.2
  • 51
    • 0037208127 scopus 로고    scopus 로고
    • Degradation of [γ]- and [α]-tocopherol and formation of 5-nitro-[γ]-tocopherol induced by peroxynitrite in liposomes and skeletal muscle
    • Brannan, R. G.; Decker, E. A. Degradation of [γ]- and [α]-tocopherol and formation of 5-nitro-[γ]-tocopherol induced by peroxynitrite in liposomes and skeletal muscle. Meat Sci. 2003, 64, 149-156.
    • (2003) Meat Sci. , vol.64 , pp. 149-156
    • Brannan, R.G.1    Decker, E.A.2
  • 52
    • 0037189879 scopus 로고    scopus 로고
    • Potential of peroxynitrite to alter the color of myoglobin in muscle foods
    • Connolly, B. J.; Brannan, R. G.; Decker, E. A. Potential of peroxynitrite to alter the color of myoglobin in muscle foods. J. Agric. Food Chem. 2002, 50, 5220-5223.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 5220-5223
    • Connolly, B.J.1    Brannan, R.G.2    Decker, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.