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Volumn 86, Issue , 2015, Pages 259-268

Bilirubin scavenges chloramines and inhibits myeloperoxidase-induced protein/lipid oxidation in physiologically relevant hyperbilirubinemic serum

Author keywords

Antioxidants; Bile pigments; Chloramines; Free radicals; Heme oxygenase; Myeloperoxidase; Protein oxidation

Indexed keywords

BILIRUBIN; CHLORAMINE DERIVATIVE; MALONALDEHYDE; PEROXIDASE;

EID: 84945285459     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2015.05.031     Document Type: Article
Times cited : (34)

References (66)
  • 1
    • 0028084319 scopus 로고
    • Association of low serum concentration of bilirubin with increased risk of coronary-artery disease
    • H.A. Schwertner, W.G. Jackson, and G. Tolan Association of low serum concentration of bilirubin with increased risk of coronary-artery disease Clin. Chem. 40 1994 18 23
    • (1994) Clin. Chem. , vol.40 , pp. 18-23
    • Schwertner, H.A.1    Jackson, W.G.2    Tolan, G.3
  • 4
    • 0038047678 scopus 로고    scopus 로고
    • Inverse relationship between serum bilirubin and atherosclerosis in men: A meta-analysis of published studies
    • L. Novotny, and L. Vitek Inverse relationship between serum bilirubin and atherosclerosis in men: a meta-analysis of published studies Exp. Biol. Med. (Maywood) 228 2003 568 571
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 568-571
    • Novotny, L.1    Vitek, L.2
  • 5
    • 84866480062 scopus 로고    scopus 로고
    • Lower carotid intima media thickness is predicted by higher serum bilirubin in both non-diabetic and type 2 diabetic subjects
    • R.P. Dullaart, P.J. Kappelle, and R. de Vries Lower carotid intima media thickness is predicted by higher serum bilirubin in both non-diabetic and type 2 diabetic subjects Clin. Chim. Acta 414 2012 161 165
    • (2012) Clin. Chim. Acta , vol.414 , pp. 161-165
    • Dullaart, R.P.1    Kappelle, P.J.2    De Vries, R.3
  • 7
    • 84899852226 scopus 로고    scopus 로고
    • Effects of serum bilirubin on atherosclerotic processes
    • S.J. Kang, C. Lee, and P. Kruzliak Effects of serum bilirubin on atherosclerotic processes Ann. Med. 46 2014 138 147
    • (2014) Ann. Med. , vol.46 , pp. 138-147
    • Kang, S.J.1    Lee, C.2    Kruzliak, P.3
  • 9
    • 79953004070 scopus 로고    scopus 로고
    • Serum bilirubin links UGT1A1∗28 polymorphism and predicts long-term cardiovascular events and mortality in chronic hemodialysis patients
    • Y.H. Chen, S.C. Hung, and D.C. Tarng Serum bilirubin links UGT1A1∗28 polymorphism and predicts long-term cardiovascular events and mortality in chronic hemodialysis patients Clin. J. Am. Soc. Nephrol. 6 2011 567 574
    • (2011) Clin. J. Am. Soc. Nephrol. , vol.6 , pp. 567-574
    • Chen, Y.H.1    Hung, S.C.2    Tarng, D.C.3
  • 11
    • 84860415023 scopus 로고    scopus 로고
    • Usefulness of serum bilirubin and cardiorespiratory fitness as predictors of mortality in men
    • R. Ajja, D.C. Lee, X. Sui, T.S. Church, and N.B. Steven Usefulness of serum bilirubin and cardiorespiratory fitness as predictors of mortality in men Am. J. Cardiol. 108 2011 1438 1442
    • (2011) Am. J. Cardiol. , vol.108 , pp. 1438-1442
    • Ajja, R.1    Lee, D.C.2    Sui, X.3    Church, T.S.4    Steven, N.B.5
  • 12
    • 84904343067 scopus 로고    scopus 로고
    • Circulating bilirubin and defense against kidney disease and cardiovascular mortality: Mechanisms contributing to protection in clinical investigations
    • A.C. Boon, A.C. Bulmer, J.S. Coombes, and R.G. Fassett Circulating bilirubin and defense against kidney disease and cardiovascular mortality: mechanisms contributing to protection in clinical investigations Am. J. Physiol. Renal Physiol. 307 2014 F123 F136
    • (2014) Am. J. Physiol. Renal Physiol. , vol.307 , pp. F123-F136
    • Boon, A.C.1    Bulmer, A.C.2    Coombes, J.S.3    Fassett, R.G.4
  • 13
    • 4644310560 scopus 로고    scopus 로고
    • Role of oxidative modifications in atherosclerosis
    • R. Stocker, and J.F. Keaney Jr. Role of oxidative modifications in atherosclerosis Physiol. Rev. 84 2004 1381 1478
    • (2004) Physiol. Rev. , vol.84 , pp. 1381-1478
    • Stocker, R.1    Keaney, J.F.2
  • 14
    • 0027490428 scopus 로고
    • Bilirubin attenuates radical-mediated damage to serum albumin
    • J. Neuzil, and R. Stocker Bilirubin attenuates radical-mediated damage to serum albumin FEBS Lett. 331 1993 281 284
    • (1993) FEBS Lett. , vol.331 , pp. 281-284
    • Neuzil, J.1    Stocker, R.2
  • 15
    • 0027293206 scopus 로고
    • Radical-induced chain oxidation of proteins and its inhibition by chain-breaking antioxidants
    • J. Neuzil, J.M. Gebicki, and R. Stocker Radical-induced chain oxidation of proteins and its inhibition by chain-breaking antioxidants Biochem. J. 293 1993 601 606
    • (1993) Biochem. J. , vol.293 , pp. 601-606
    • Neuzil, J.1    Gebicki, J.M.2    Stocker, R.3
  • 17
    • 0028239795 scopus 로고
    • Free and albumin-bound bilirubin are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low density lipoprotein lipid peroxidation
    • J. Neuzil, and R. Stocker Free and albumin-bound bilirubin are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low density lipoprotein lipid peroxidation J. Biol. Chem. 269 1994 16712 16719
    • (1994) J. Biol. Chem. , vol.269 , pp. 16712-16719
    • Neuzil, J.1    Stocker, R.2
  • 18
    • 0028313015 scopus 로고
    • Unconjugated bilirubin inhibits the oxidation of human low density lipoprotein better than Trolox
    • T.W. Wu, K.P. Fung, and C.C. Yang Unconjugated bilirubin inhibits the oxidation of human low density lipoprotein better than Trolox Life Sci. 54 1994 P477 P481
    • (1994) Life Sci. , vol.54 , pp. P477-P481
    • Wu, T.W.1    Fung, K.P.2    Yang, C.C.3
  • 19
    • 0024601475 scopus 로고
    • Antioxidant properties of conjugated bilirubin and biliverdin: Biologically relevant scavenging of hypochlorous acid
    • R. Stocker, and E. Peterhans Antioxidant properties of conjugated bilirubin and biliverdin: biologically relevant scavenging of hypochlorous acid Free Radic. Res. Commun. 6 1989 57 66
    • (1989) Free Radic. Res. Commun. , vol.6 , pp. 57-66
    • Stocker, R.1    Peterhans, E.2
  • 20
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • M.J. Davies, C.L. Hawkins, D.I. Pattison, and M.D. Rees Mammalian heme peroxidases: from molecular mechanisms to health implications Antioxid. Redox Signaling 10 2008 1199 1234
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 22
    • 66349123572 scopus 로고    scopus 로고
    • Modified lipoproteins, and atherogenesis
    • S.J. Nicholls, and Hazen S.L. Myeloperoxidase modified lipoproteins, and atherogenesis J. Lipid Res 50 Suppl 2009 S346 S351
    • (2009) J. Lipid Res , vol.50 , pp. S346-S351
    • Nicholls, S.J.1    Myeloperoxidase, H.S.L.2
  • 24
    • 0028292033 scopus 로고
    • Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions
    • A. Daugherty, J.L. Dunn, D.L. Rateri, and J.W. Heinecke Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions J. Clin. Invest. 94 1994 437 444
    • (1994) J. Clin. Invest. , vol.94 , pp. 437-444
    • Daugherty, A.1    Dunn, J.L.2    Rateri, D.L.3    Heinecke, J.W.4
  • 25
    • 0001059250 scopus 로고    scopus 로고
    • 2/halide system in human atherosclerotic lesions: Colocalization of myeloperoxidase and hypochlorite-modified proteins
    • 2/halide system in human atherosclerotic lesions: colocalization of myeloperoxidase and hypochlorite-modified proteins Eur. J. Biochem. 267 2000 4495 4503
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4495-4503
    • Malle, E.1    Waeg, G.2    Schreiber, R.3    Grone, E.F.4    Sattler, W.5    Grone, H.J.6
  • 26
    • 84953335312 scopus 로고    scopus 로고
    • Increased myeloperoxidase expression is associated with increase in intra-plaque hemorrhage, iron content, inflammation and neovascularization in diabetic atherosclerosis: Implications for plaque progression
    • R. Purushothaman, M. Purushothaman, L.A. Carlos, A. Tarricone, M. Vasquez, P. Krishnan, A. Kini, S. Sharma, V. Fuster, and R.M. Pedro Increased myeloperoxidase expression is associated with increase in intra-plaque hemorrhage, iron content, inflammation and neovascularization in diabetic atherosclerosis: implications for plaque progression J. Cardiovasc. Dis. Diagn 1 2013 118
    • (2013) J. Cardiovasc. Dis. Diagn , vol.1 , pp. 118
    • Purushothaman, R.1    Purushothaman, M.2    Carlos, L.A.3    Tarricone, A.4    Vasquez, M.5    Krishnan, P.6    Kini, A.7    Sharma, S.8    Fuster, V.9    Pedro, R.M.10
  • 27
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • D.I. Pattison, and M.J. Davies Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases Curr. Med. Chem. 13 2006 3271 3290
    • (2006) Curr. Med. Chem. , vol.13 , pp. 3271-3290
    • Pattison, D.I.1    Davies, M.J.2
  • 29
    • 0033151902 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of proteins in plasma: Formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation
    • C.L. Hawkins, and M.J. Davies Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation Biochem. J. 340 1999 539 548
    • (1999) Biochem. J. , vol.340 , pp. 539-548
    • Hawkins, C.L.1    Davies, M.J.2
  • 30
    • 0033136258 scopus 로고    scopus 로고
    • Secondary radicals derived from chloramines of apolipoprotein B-100 contribute to HOCl-induced lipid peroxidation of low-density lipoproteins
    • L.J. Hazell, M.J. Davies, and R. Stocker Secondary radicals derived from chloramines of apolipoprotein B-100 contribute to HOCl-induced lipid peroxidation of low-density lipoproteins Biochem. J. 339 1999 489 495
    • (1999) Biochem. J. , vol.339 , pp. 489-495
    • Hazell, L.J.1    Davies, M.J.2    Stocker, R.3
  • 31
    • 4544222836 scopus 로고
    • Antioxidant properties of bilirubin and biliverdin
    • O. Hayaishi, Elsevier San Diego Proceedings of the 4th Biennial General Meeting of the Society for Free Radical Research, Kyoto, Japan
    • R. Stocker, A. Lai, E. Peterhans, and B.N. Ames Antioxidant properties of bilirubin and biliverdin O. Hayaishi, Medical, Biochemical, and Chemical Aspects of Free Radicals Vol. 1 1988 Elsevier San Diego 465 468 Proceedings of the 4th Biennial General Meeting of the Society for Free Radical Research, Kyoto, Japan
    • (1988) Medical, Biochemical, and Chemical Aspects of Free Radicals , vol.1 , pp. 465-468
    • Stocker, R.1    Lai, A.2    Peterhans, E.3    Ames, B.N.4
  • 32
    • 0036498731 scopus 로고    scopus 로고
    • Frequencies of UDP-glucuronosyltransferase 1 (UGT1A1) gene promoter polymorphisms among distinct ethnic groups from Brazil
    • K.Y. Fertrin, M.S. Goncalves, S.T. Saad, and F.F. Costa Frequencies of UDP-glucuronosyltransferase 1 (UGT1A1) gene promoter polymorphisms among distinct ethnic groups from Brazil Am. J. Med. Genet. 108 2002 117 119
    • (2002) Am. J. Med. Genet. , vol.108 , pp. 117-119
    • Fertrin, K.Y.1    Goncalves, M.S.2    Saad, S.T.3    Costa, F.F.4
  • 33
    • 84861047353 scopus 로고    scopus 로고
    • Reduced circulating oxidized LDL is associated with hypocholesterolemia and enhanced thiol status in Gilbert syndrome
    • A.C. Boon, C.L. Hawkins, K. Bisht, J.S. Coombes, B. Bakrania, K.H. Wagner, and A.C. Bulmer Reduced circulating oxidized LDL is associated with hypocholesterolemia and enhanced thiol status in Gilbert syndrome Free Radic. Biol. Med. 52 2012 2120 2127
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 2120-2127
    • Boon, A.C.1    Hawkins, C.L.2    Bisht, K.3    Coombes, J.S.4    Bakrania, B.5    Wagner, K.H.6    Bulmer, A.C.7
  • 34
    • 0030586361 scopus 로고    scopus 로고
    • The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": The FRAP assay
    • I.F. Benzie, and J.J. Strain The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": the FRAP assay Anal. Biochem. 239 1996 70 76
    • (1996) Anal. Biochem. , vol.239 , pp. 70-76
    • Benzie, I.F.1    Strain, J.J.2
  • 35
    • 47649112255 scopus 로고    scopus 로고
    • Improved resistance to serum oxidation in Gilbert's syndrome: A mechanism for cardiovascular protection
    • A.C. Bulmer, J.T. Blanchfield, I. Toth, R.G. Fassett, and J.S. Coornbes Improved resistance to serum oxidation in Gilbert's syndrome: a mechanism for cardiovascular protection Atherosclerosis 199 2008 390 396
    • (2008) Atherosclerosis , vol.199 , pp. 390-396
    • Bulmer, A.C.1    Blanchfield, J.T.2    Toth, I.3    Fassett, R.G.4    Coornbes, J.S.5
  • 37
    • 53549122736 scopus 로고    scopus 로고
    • Identification of plasma proteins that are susceptible to thiol oxidation by hypochlorous acid and N-chloramines
    • F.A. Summers, P.E. Morgan, M.J. Davies, and C.L. Hawkins Identification of plasma proteins that are susceptible to thiol oxidation by hypochlorous acid and N-chloramines Chem. Res. Toxicol. 21 2008 1832 1840
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 1832-1840
    • Summers, F.A.1    Morgan, P.E.2    Davies, M.J.3    Hawkins, C.L.4
  • 39
    • 0029867381 scopus 로고    scopus 로고
    • Automated high-performance liquid chromatographic separation with spectrofluorometric detection of a malondialdehyde-thiobarbituric acid adduct in plasma
    • D. Londero, and P. Lo Greco Automated high-performance liquid chromatographic separation with spectrofluorometric detection of a malondialdehyde-thiobarbituric acid adduct in plasma J. Chromatogr. A 729 1996 207 210
    • (1996) J. Chromatogr. A , vol.729 , pp. 207-210
    • Londero, D.1    Lo Greco, P.2
  • 40
    • 84889585312 scopus 로고    scopus 로고
    • Protein oxidative modifications: Beneficial roles in disease and health. J. Biochem
    • Z. Cai, and L.J. Yan Protein oxidative modifications: beneficial roles in disease and health. J. Biochem Pharmacol. Res. 1 2013 15 26
    • (2013) Pharmacol. Res. , vol.1 , pp. 15-26
    • Cai, Z.1    Yan, L.J.2
  • 42
    • 1842685103 scopus 로고    scopus 로고
    • Markers of protein oxidation: Different oxidants give rise to variable yields of bound and released carbonyl products
    • H.A. Headlam, and M.J. Davies Markers of protein oxidation: different oxidants give rise to variable yields of bound and released carbonyl products Free Radic. Biol. Med. 36 2004 1175 1184
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1175-1184
    • Headlam, H.A.1    Davies, M.J.2
  • 43
    • 33646826643 scopus 로고
    • Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid
    • E. Malle, G. Marsche, J. Arnhold, and M.J. Davies Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid Biochim. Biophys. Acta 392-415 1761 2006
    • (1761) Biochim. Biophys. Acta , vol.392 , pp. 2006
    • Malle, E.1    Marsche, G.2    Arnhold, J.3    Davies, M.J.4
  • 44
    • 79951958873 scopus 로고    scopus 로고
    • Oxidative stress biomarkers as predictors of cardiovascular disease
    • N.A. Strobel, R.G. Fassett, S.A. Marsh, and J.S. Coombes Oxidative stress biomarkers as predictors of cardiovascular disease Int. J. Cardiol. 147 2011 191 201
    • (2011) Int. J. Cardiol. , vol.147 , pp. 191-201
    • Strobel, N.A.1    Fassett, R.G.2    Marsh, S.A.3    Coombes, J.S.4
  • 48
    • 0035864610 scopus 로고    scopus 로고
    • Association of plasma bilirubin with coronary heart disease and segregation of bilirubin as a major gene trait: The NHLBI family heart study
    • S.C. Hunt, F. Kronenberg, J.H. Eckfeldt, P.N. Hopkins, R.H. Myers, and G. Heiss Association of plasma bilirubin with coronary heart disease and segregation of bilirubin as a major gene trait: the NHLBI family heart study Atherosclerosis 154 2001 747 754
    • (2001) Atherosclerosis , vol.154 , pp. 747-754
    • Hunt, S.C.1    Kronenberg, F.2    Eckfeldt, J.H.3    Hopkins, P.N.4    Myers, R.H.5    Heiss, G.6
  • 49
  • 50
    • 0027301238 scopus 로고
    • The oxidation of blood plasma and low density lipoprotein components by chemically generated singlet oxygen
    • J.R. Wagner, P.A. Motchnik, R. Stocker, H. Sies, and B.N. Ames The oxidation of blood plasma and low density lipoprotein components by chemically generated singlet oxygen J. Biol. Chem. 268 1993 18502 18506
    • (1993) J. Biol. Chem. , vol.268 , pp. 18502-18506
    • Wagner, J.R.1    Motchnik, P.A.2    Stocker, R.3    Sies, H.4    Ames, B.N.5
  • 51
    • 0024588311 scopus 로고
    • Synergistic interaction between Vitamin E and the bile pigments bilirubin and biliverdin
    • R. Stocker, and E. Peterhans Synergistic interaction between vitamin E and the bile pigments bilirubin and biliverdin Biochim. Biophys. Acta 1002 1989 238 244
    • (1989) Biochim. Biophys. Acta , vol.1002 , pp. 238-244
    • Stocker, R.1    Peterhans, E.2
  • 52
    • 0034468846 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of thiols: Formation of thiyl radicals and the role of sulfenyl chlorides as intermediates
    • M.J. Davies, and C.L. Hawkins Hypochlorite-induced oxidation of thiols: formation of thiyl radicals and the role of sulfenyl chlorides as intermediates Free Radic. Res. 33 2000 719 729
    • (2000) Free Radic. Res. , vol.33 , pp. 719-729
    • Davies, M.J.1    Hawkins, C.L.2
  • 53
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: Formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
    • C.L. Hawkins, and M.J. Davies Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation Biochem. J. 332 1998 617 625
    • (1998) Biochem. J. , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 54
    • 0034861165 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to nucleosides: Formation of chloramines and nitrogen-centered radicals
    • C.L. Hawkins, and M.J. Davies Hypochlorite-induced damage to nucleosides: formation of chloramines and nitrogen-centered radicals Chem. Res. Toxicol. 14 2001 1071 1081
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1071-1081
    • Hawkins, C.L.1    Davies, M.J.2
  • 55
    • 0033065908 scopus 로고    scopus 로고
    • Threshold concentration of unbound bilirubin to induce neurological deficits in a patient with type I Crigler-Najjar syndrome
    • H. Ihara, N. Hashizume, N. Shimizu, and T. Aoki Threshold concentration of unbound bilirubin to induce neurological deficits in a patient with type I Crigler-Najjar syndrome Ann. Clin. Biochem. 36 1999 347 352
    • (1999) Ann. Clin. Biochem. , vol.36 , pp. 347-352
    • Ihara, H.1    Hashizume, N.2    Shimizu, N.3    Aoki, T.4
  • 56
    • 84875750146 scopus 로고    scopus 로고
    • Bilirubin and beyond: A review of lipid status in Gilbert's syndrome and its relevance to cardiovascular disease protection
    • A.C. Bulmer, H.J. Verkade, and K.H. Wagner Bilirubin and beyond: a review of lipid status in Gilbert's syndrome and its relevance to cardiovascular disease protection Prog. Lipid Res. 52 2013 193 205
    • (2013) Prog. Lipid Res. , vol.52 , pp. 193-205
    • Bulmer, A.C.1    Verkade, H.J.2    Wagner, K.H.3
  • 57
    • 1342267473 scopus 로고    scopus 로고
    • Further evidence of altered redox status of hyperbilirubinaemic patients: Role of bilirubin in Gilbert syndrome
    • K. Hagymási, I. Kocsis, G. Lengyel, P. Sipos, J. Fehér, and A. Blázovics Further evidence of altered redox status of hyperbilirubinaemic patients: role of bilirubin in Gilbert syndrome Acta Biol. Szeged 47 2003 131 134
    • (2003) Acta Biol. Szeged , vol.47 , pp. 131-134
    • Hagymási, K.1    Kocsis, I.2    Lengyel, G.3    Sipos, P.4    Fehér, J.5    Blázovics, A.6
  • 58
    • 0032570808 scopus 로고    scopus 로고
    • Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes: Mechanistic studies identifying labile intermediates along the reaction pathway
    • S.L. Hazen, A. d'Avignon, M.M. Anderson, F.F. Hsu, and J.W. Heinecke Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes: mechanistic studies identifying labile intermediates along the reaction pathway J. Biol. Chem. 273 1998 4997 5005
    • (1998) J. Biol. Chem. , vol.273 , pp. 4997-5005
    • Hazen, S.L.1    D'Avignon, A.2    Anderson, M.M.3    Hsu, F.F.4    Heinecke, J.W.5
  • 60
    • 0034524859 scopus 로고    scopus 로고
    • Human studies related to protein oxidation: Protein carbonyl content as a marker of damage
    • M. Chevion, E. Berenshtein, and E.R. Stadtman Human studies related to protein oxidation: protein carbonyl content as a marker of damage Free Radic. Res 33 Suppl 2000 S99 S108
    • (2000) Free Radic. Res , vol.33 , pp. S99-S108
    • Chevion, M.1    Berenshtein, E.2    Stadtman, E.R.3
  • 62
    • 0027516393 scopus 로고
    • Oxidation of low-density lipoprotein with hypochlorite causes transformation of the lipoprotein into a high-uptake form for macrophages
    • L.J. Hazell, and R. Stocker Oxidation of low-density lipoprotein with hypochlorite causes transformation of the lipoprotein into a high-uptake form for macrophages Biochem. J. 290 1993 165 172
    • (1993) Biochem. J. , vol.290 , pp. 165-172
    • Hazell, L.J.1    Stocker, R.2
  • 63
  • 65
    • 33746911144 scopus 로고    scopus 로고
    • Lipid and protein oxidation and antioxidant status in patients with angiographically proven coronary artery disease
    • Z. Serdar, K. Aslan, M. Dirican, E. Sarandol, D. Yesilbursa, and A. Serdar Lipid and protein oxidation and antioxidant status in patients with angiographically proven coronary artery disease Clin. Biochem. 39 2006 794 803
    • (2006) Clin. Biochem. , vol.39 , pp. 794-803
    • Serdar, Z.1    Aslan, K.2    Dirican, M.3    Sarandol, E.4    Yesilbursa, D.5    Serdar, A.6
  • 66
    • 81355143343 scopus 로고    scopus 로고
    • Bile pigment pharmacokinetics and absorption in the rat: Therapeutic potential for enteral administration
    • A.C. Bulmer, J.S. Coombes, J.T. Blanchfield, I. Toth, R.G. Fassett, and S.M. Taylor Bile pigment pharmacokinetics and absorption in the rat: therapeutic potential for enteral administration Br. J. Pharmacol. 164 2011 1857 1870
    • (2011) Br. J. Pharmacol. , vol.164 , pp. 1857-1870
    • Bulmer, A.C.1    Coombes, J.S.2    Blanchfield, J.T.3    Toth, I.4    Fassett, R.G.5    Taylor, S.M.6


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