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Volumn , Issue , 2010, Pages 76-104

Heme proteins and oxidation in fresh and processed meats

Author keywords

Blood; Discoloration; Hemoglobin; Myoglobin; Quality deterioration; Rancidity

Indexed keywords


EID: 84864684763     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1533/9780857090447.1.77     Document Type: Chapter
Times cited : (25)

References (115)
  • 1
    • 0033593463 scopus 로고    scopus 로고
    • Reactions of sperm whale myoglobin with hydrogen peroxide. Effects of distal pocket mutations on the formation and stability of the ferryl intermediate
    • Alayash A.I., Brockner Ryan B.A., Eich R.F., Olson J.S., Cashon R.E. Reactions of sperm whale myoglobin with hydrogen peroxide. Effects of distal pocket mutations on the formation and stability of the ferryl intermediate. J. Biol. Chem., 1999, 274:2029-2037.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2029-2037
    • Alayash, A.I.1    Brockner Ryan, B.A.2    Eich, R.F.3    Olson, J.S.4    Cashon, R.E.5
  • 4
    • 65249151456 scopus 로고    scopus 로고
    • Structural analysis of fish versus mammalian hemoglobins: effects of the heme pocket environment on autooxidation and hemin loss rates
    • Aranda R., He C., Worley C.E., Levin E., Li R., Olson J.S., Phillips G.N., Richards M.P. Structural analysis of fish versus mammalian hemoglobins: effects of the heme pocket environment on autooxidation and hemin loss rates. Proteins 2009, 75:217-230.
    • (2009) Proteins , vol.75 , pp. 217-230
    • Aranda, R.1    He, C.2    Worley, C.E.3    Levin, E.4    Li, R.5    Olson, J.S.6    Phillips, G.N.7    Richards, M.P.8
  • 5
    • 39149099088 scopus 로고    scopus 로고
    • Tocopherols and tocotrienols in membranes: A critical review
    • Atkinson J., Epand R.F., Epand R.M. Tocopherols and tocotrienols in membranes: A critical review. Free Radic. Biol. Med. 2008, 44:739-764.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 739-764
    • Atkinson, J.1    Epand, R.F.2    Epand, R.M.3
  • 6
    • 0026318447 scopus 로고
    • Hema possible physiological mediator of low density lipoprotein oxidation and endothelial injury
    • Balla G., Jacob H.S., Eaton J.W., Belcher J.D., Vercellotti G.M. Hema possible physiological mediator of low density lipoprotein oxidation and endothelial injury. Arterioscler. Thromb. 1991, 11:1700-1711.
    • (1991) Arterioscler. Thromb. , vol.11 , pp. 1700-1711
    • Balla, G.1    Jacob, H.S.2    Eaton, J.W.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 7
    • 9544238749 scopus 로고
    • Study of hematin-globin linkage. Determination of equilibrium constants
    • Banerjee R. Study of hematin-globin linkage. Determination of equilibrium constants. Biochem. Biophys. Res. Commun. 1962, 8:114-119.
    • (1962) Biochem. Biophys. Res. Commun. , vol.8 , pp. 114-119
    • Banerjee, R.1
  • 9
    • 0001748739 scopus 로고    scopus 로고
    • Prooxidative activity of myoglobin species in linoleic acid emulsions
    • Baron C.P., Skibsted L.H., Andersen H.J. Prooxidative activity of myoglobin species in linoleic acid emulsions. J. Agric. Food Chem. 1997, 45:1704-1710.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1704-1710
    • Baron, C.P.1    Skibsted, L.H.2    Andersen, H.J.3
  • 10
    • 0034652634 scopus 로고    scopus 로고
    • Peroxidation of linoleate at physiological pH: hemichrome formation by substrate binding protects against metmyoglobin activation by hydrogen peroxide
    • Baron C.P., Skibsted L.H., Andersen H.J. Peroxidation of linoleate at physiological pH: hemichrome formation by substrate binding protects against metmyoglobin activation by hydrogen peroxide. Free Radical Biol. Med. 2000, 28:549-558.
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 549-558
    • Baron, C.P.1    Skibsted, L.H.2    Andersen, H.J.3
  • 11
    • 33745650662 scopus 로고    scopus 로고
    • Industrial packaging developments for the global meat market
    • Belcher J.N. Industrial packaging developments for the global meat market. Meat Sci. 2006, 74:143-148.
    • (2006) Meat Sci. , vol.74 , pp. 143-148
    • Belcher, J.N.1
  • 12
    • 0014985250 scopus 로고
    • Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood
    • Binotti I., Giovenco S., Giardina B., Antonini E., Brunori M., Wyman J. Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood. Arch. Biochem. Biophys. 1971, 142:274-280.
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 274-280
    • Binotti, I.1    Giovenco, S.2    Giardina, B.3    Antonini, E.4    Brunori, M.5    Wyman, J.6
  • 13
    • 0036096132 scopus 로고    scopus 로고
    • Oxidized phospholipids stimulate tissue factor expression in human endothelial cells via activation of ERK/EGR-1 and Ca(++)/NFAT
    • Bochkov V.N., Mechtcheriakova D., Lucerna M., Huber J., R M., Graier W.F., Hofer E., Binder B.R., Leitinger N. Oxidized phospholipids stimulate tissue factor expression in human endothelial cells via activation of ERK/EGR-1 and Ca(++)/NFAT. Blood 2002, 99:199-206.
    • (2002) Blood , vol.99 , pp. 199-206
    • Bochkov, V.N.1    Mechtcheriakova, D.2    Lucerna, M.3    Huber, J.R.M.4    Graier, W.F.5    Hofer, E.6    Binder, B.R.7    Leitinger, N.8
  • 14
    • 0023787317 scopus 로고
    • Reductive release of ferritin iron: a kinetic assay
    • Boyer R.F., Grabill T.W., Petrovich R.M. Reductive release of ferritin iron: a kinetic assay. Anal. Biochem. 1988, 174:17-22.
    • (1988) Anal. Biochem. , vol.174 , pp. 17-22
    • Boyer, R.F.1    Grabill, T.W.2    Petrovich, R.M.3
  • 16
    • 33746701292 scopus 로고    scopus 로고
    • Nitrite in nitric oxide biology: cause or consequence? A systems-based review
    • Bryan N.S. Nitrite in nitric oxide biology: cause or consequence? A systems-based review. Free Radic. Biol. Med. 2006, 41:691-701.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 691-701
    • Bryan, N.S.1
  • 18
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol, and ascorbate
    • Buettner G.R. The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol, and ascorbate. Arch. Biochem. Biophys. 1993, 300:535-543.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 19
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn H.F., Jandl J.H. Exchange of heme among hemoglobins and between hemoglobin and albumin. J. Biol. Chem. 1968, 243:465-475.
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 20
    • 0030819158 scopus 로고    scopus 로고
    • Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures
    • Cashon R.E., Vayda M.E., Sidell B.D. Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1997, 117:613-620.
    • (1997) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.117 , pp. 613-620
    • Cashon, R.E.1    Vayda, M.E.2    Sidell, B.D.3
  • 21
    • 0002050034 scopus 로고    scopus 로고
    • Residual nitrite in cured meat
    • Cassens R.G. Residual nitrite in cured meat. Food Technol. 1997, 51:53-55.
    • (1997) Food Technol. , vol.51 , pp. 53-55
    • Cassens, R.G.1
  • 27
    • 0032513024 scopus 로고    scopus 로고
    • Immobilized apo-myoglobin, a new stable reagent for measuring rates of heme dissociation from hemoglobin
    • Gattoni M., Boffi A., Chiancone E. Immobilized apo-myoglobin, a new stable reagent for measuring rates of heme dissociation from hemoglobin. FEBS Lett. 1998, 424:275-278.
    • (1998) FEBS Lett. , vol.424 , pp. 275-278
    • Gattoni, M.1    Boffi, A.2    Chiancone, E.3
  • 28
    • 77955260149 scopus 로고    scopus 로고
    • Factors affecting lipid oxidation in breast and thigh muscle from chicken, turkey and duck
    • doi: 10.1111/j.1745-4514.2010.00341.x
    • Gong Y., Parker R.S., Richards M.P. Factors affecting lipid oxidation in breast and thigh muscle from chicken, turkey and duck. J. Food Biochem. 2010, doi: 10.1111/j.1745-4514.2010.00341.x.
    • (2010) J. Food Biochem.
    • Gong, Y.1    Parker, R.S.2    Richards, M.P.3
  • 29
    • 38049144598 scopus 로고    scopus 로고
    • A novel function of red wine polyphenols in humans: prevention of absorption of cytotoxic lipid peroxidation products
    • Gorelik S., Ligumsky M., Kohen R., Kanner J. A novel function of red wine polyphenols in humans: prevention of absorption of cytotoxic lipid peroxidation products. Faseb J. 2008, 22:41-46.
    • (2008) Faseb J. , vol.22 , pp. 41-46
    • Gorelik, S.1    Ligumsky, M.2    Kohen, R.3    Kanner, J.4
  • 31
    • 0037794084 scopus 로고    scopus 로고
    • Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron
    • Grinshtein N., Bamm V.V., Tsemakhovich V.A., Shaklai N. Mechanism of low-density lipoprotein oxidation by hemoglobin-derived iron. Biochemistry 2003, 42:6977-6985.
    • (2003) Biochemistry , vol.42 , pp. 6977-6985
    • Grinshtein, N.1    Bamm, V.V.2    Tsemakhovich, V.A.3    Shaklai, N.4
  • 32
    • 33751241425 scopus 로고    scopus 로고
    • Mechanisms of heme protein-mediated lipid oxidation using hemoglobin and myoglobin variants in raw and heated washed muscle
    • Grunwald E.W., Richards M.P. Mechanisms of heme protein-mediated lipid oxidation using hemoglobin and myoglobin variants in raw and heated washed muscle. J. Agric. Food Chem. 2006, 54:8271-8280.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 8271-8280
    • Grunwald, E.W.1    Richards, M.P.2
  • 33
    • 33745739158 scopus 로고    scopus 로고
    • Studies with myoglobin variants indicate that released hemin is the primary promoter of lipid oxidation in washed fish muscle
    • Grunwald E.W., Richards M.P. Studies with myoglobin variants indicate that released hemin is the primary promoter of lipid oxidation in washed fish muscle. J. Agric. Food Chem. 2006, 54:4452-4460.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 4452-4460
    • Grunwald, E.W.1    Richards, M.P.2
  • 37
    • 0029737668 scopus 로고    scopus 로고
    • Structural factors governing hemin dissociation from metmyoglobin
    • Hargrove M.S., Wilkinson A.J., Olson J.S. Structural factors governing hemin dissociation from metmyoglobin. Biochemistry 1996, 35:11300-11309.
    • (1996) Biochemistry , vol.35 , pp. 11300-11309
    • Hargrove, M.S.1    Wilkinson, A.J.2    Olson, J.S.3
  • 38
    • 0030814099 scopus 로고    scopus 로고
    • Quaternary structure regulates hemin dissociation from human hemoglobin
    • Hargrove M.S., Whitaker T., Olson J.S., Vali R.J., Mathews A.J. Quaternary structure regulates hemin dissociation from human hemoglobin. J. Biol. Chem. 1997, 272:17385-17389.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17385-17389
    • Hargrove, M.S.1    Whitaker, T.2    Olson, J.S.3    Vali, R.J.4    Mathews, A.J.5
  • 40
    • 0000441787 scopus 로고
    • Influence of heme pigments, nitrite, and non-heme iron on development of warmed-over flavor (WOF) in cooked meats
    • Igene J.O., King J.A., Pearson A.M., Gray J.I. Influence of heme pigments, nitrite, and non-heme iron on development of warmed-over flavor (WOF) in cooked meats. J. Agric. Food Chem. 1979, 27:838-842.
    • (1979) J. Agric. Food Chem. , vol.27 , pp. 838-842
    • Igene, J.O.1    King, J.A.2    Pearson, A.M.3    Gray, J.I.4
  • 41
    • 0000171205 scopus 로고
    • Evaluation of 2-thiobarbituric acid reactive substances (TBRS) in relation to warmed-over flavor (WOF) development in cooked chicken
    • Igene J.O., Yamauchi K., Pearson A.M., Gray J.I., Aust S.D. Evaluation of 2-thiobarbituric acid reactive substances (TBRS) in relation to warmed-over flavor (WOF) development in cooked chicken. J. Agric. Food Chem. 1985, 33:364-367.
    • (1985) J. Agric. Food Chem. , vol.33 , pp. 364-367
    • Igene, J.O.1    Yamauchi, K.2    Pearson, A.M.3    Gray, J.I.4    Aust, S.D.5
  • 42
    • 0000522990 scopus 로고
    • Catalysts of lipid oxidation in meat products
    • Johns A.M., Birkinshaw L.H., Ledward D.A. Catalysts of lipid oxidation in meat products. Meat Sci. 1989, 25:209-220.
    • (1989) Meat Sci. , vol.25 , pp. 209-220
    • Johns, A.M.1    Birkinshaw, L.H.2    Ledward, D.A.3
  • 43
    • 0021667281 scopus 로고
    • Biosynthesis of rainbow trout (Salmo gairdnerii) hemoglobins in vitro
    • Jolly J.K., Taketa F. Biosynthesis of rainbow trout (Salmo gairdnerii) hemoglobins in vitro. Comp. Biochem. Physiol. B 1984, 79:537-540.
    • (1984) Comp. Biochem. Physiol. B , vol.79 , pp. 537-540
    • Jolly, J.K.1    Taketa, F.2
  • 44
    • 43949154597 scopus 로고
    • Oxidative processes in meat and meat-products - quality implications
    • Kanner J. Oxidative processes in meat and meat-products - quality implications. Meat Sci. 1994, 36:169-189.
    • (1994) Meat Sci. , vol.36 , pp. 169-189
    • Kanner, J.1
  • 45
    • 0022001719 scopus 로고
    • Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin
    • Kanner J., Harel S. Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Arch. Biochem. Biophys. 1985, 237:314-321.
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 314-321
    • Kanner, J.1    Harel, S.2
  • 46
    • 84987278720 scopus 로고
    • Prooxidant and antioxidant effect of ascorbic acid and metal salts in beta carotene-linoleate model system
    • Kanner J., Mendel H. Prooxidant and antioxidant effect of ascorbic acid and metal salts in beta carotene-linoleate model system. J. Food Sci. 1977, 42:60-64.
    • (1977) J. Food Sci. , vol.42 , pp. 60-64
    • Kanner, J.1    Mendel, H.2
  • 47
    • 33845279417 scopus 로고
    • Catalytic 'free' iron ions in muscle foods
    • Kanner J., Hazan B., Doll L. Catalytic 'free' iron ions in muscle foods. J. Agric. Food Chem. 1988, 36:412-415.
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 412-415
    • Kanner, J.1    Hazan, B.2    Doll, L.3
  • 49
    • 31344462066 scopus 로고    scopus 로고
    • Immuno-spin trapping of hemoglobin and myoglobin radicals derived from nitrite-mediated oxidation
    • Keszler A., Mason R.P., Hogg N. Immuno-spin trapping of hemoglobin and myoglobin radicals derived from nitrite-mediated oxidation. Free Radic. Biol. Med. 2006, 40:507-515.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 507-515
    • Keszler, A.1    Mason, R.P.2    Hogg, N.3
  • 51
    • 0001748740 scopus 로고    scopus 로고
    • Effect of heat denaturation on the pro-oxidative activity of metmyoglobin in linoleic acid emulsions
    • Kristensen L., Andersen H.J. Effect of heat denaturation on the pro-oxidative activity of metmyoglobin in linoleic acid emulsions. J. Agric. Food Chem. 1997, 45:7-13.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 7-13
    • Kristensen, L.1    Andersen, H.J.2
  • 52
    • 64349083819 scopus 로고    scopus 로고
    • Ability of dietary antioxidants to affect lipid oxidation of cooked turkey meat in a simulated stomach and blood lipids after a meal
    • Kuffa M., Priesbe T.J., Krueger C.G., Reed J.D., Richards M.P. Ability of dietary antioxidants to affect lipid oxidation of cooked turkey meat in a simulated stomach and blood lipids after a meal. J. Funct. Foods 2009, 1:208-216.
    • (2009) J. Funct. Foods , vol.1 , pp. 208-216
    • Kuffa, M.1    Priesbe, T.J.2    Krueger, C.G.3    Reed, J.D.4    Richards, M.P.5
  • 53
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • Kumar S., Bandyopadhyay U. Free heme toxicity and its detoxification systems in human. Toxicol. Lett. 2005, 157:175-188.
    • (2005) Toxicol. Lett. , vol.157 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 55
    • 84985280878 scopus 로고
    • Metmyoglobin formation in beef stored in carbon dioxide enriched and oxygen depleted atmospheres
    • Ledward D.A. Metmyoglobin formation in beef stored in carbon dioxide enriched and oxygen depleted atmospheres. J. Food Sci. 1970, 35:33-37.
    • (1970) J. Food Sci. , vol.35 , pp. 33-37
    • Ledward, D.A.1
  • 56
    • 0035874967 scopus 로고    scopus 로고
    • Vitamin C-induced decomposition of lipid hydroperoxides to endogenous genotoxins
    • Lee S.H., Oe T., Blair I.A. Vitamin C-induced decomposition of lipid hydroperoxides to endogenous genotoxins. Science 2001, 292:2083-2086.
    • (2001) Science , vol.292 , pp. 2083-2086
    • Lee, S.H.1    Oe, T.2    Blair, I.A.3
  • 57
    • 41149156956 scopus 로고    scopus 로고
    • Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links
    • Lund M.N., Luxford C., Skibsted L.H., Davies M.J. Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links. Biochem. J 2008, 410:565-574.
    • (2008) Biochem. J , vol.410 , pp. 565-574
    • Lund, M.N.1    Luxford, C.2    Skibsted, L.H.3    Davies, M.J.4
  • 59
    • 0032584670 scopus 로고    scopus 로고
    • Normal and abnormal protein subunit interactions in hemoglobins
    • Manning J.M., Dumoulin A., Li X., Manning L.R. Normal and abnormal protein subunit interactions in hemoglobins. J. Biol. Chem. 1998, 273:19359-19362.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19359-19362
    • Manning, J.M.1    Dumoulin, A.2    Li, X.3    Manning, L.R.4
  • 61
    • 0038880574 scopus 로고
    • The role of tocopherol content in the comparative stability of chicken and turkey fat
    • Mecchi E.P., Pool M.F., Behman G.A., Hamachi M., Klose A.A. The role of tocopherol content in the comparative stability of chicken and turkey fat. Poult. Sci. 1956, 35:1238-1246.
    • (1956) Poult. Sci. , vol.35 , pp. 1238-1246
    • Mecchi, E.P.1    Pool, M.F.2    Behman, G.A.3    Hamachi, M.4    Klose, A.A.5
  • 62
    • 0035384677 scopus 로고    scopus 로고
    • Mechanism of oxidation of oxymyoglobin by copper ions: comparison of sperm whale, horse, and pig myoglobins
    • Moiseeva S.A., Postnikova G.B. Mechanism of oxidation of oxymyoglobin by copper ions: comparison of sperm whale, horse, and pig myoglobins. Biochemistry (Mosc) 2001, 66:780-787.
    • (2001) Biochemistry (Mosc) , vol.66 , pp. 780-787
    • Moiseeva, S.A.1    Postnikova, G.B.2
  • 63
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide
    • Nagababu E., Rifkind J.M. Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide. Biochem. Biophys. Res. Commun. 1998, 247:592-596.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 64
    • 7244240720 scopus 로고    scopus 로고
    • Heme degradation by reactive oxygen species
    • Nagababu E., Rifkind J.M. Heme degradation by reactive oxygen species. Antioxid. Redox Signal 2004, 6:967-978.
    • (2004) Antioxid. Redox Signal , vol.6 , pp. 967-978
    • Nagababu, E.1    Rifkind, J.M.2
  • 65
    • 27744462839 scopus 로고    scopus 로고
    • Oxidation of hemoglobin by lipid hydroperoxide associated with low-density lipoprotein (LDL) and increased cytotoxic effect by LDL oxidation in heme oxygenase-1 (HO-1) deficiency
    • Nagy E., Jeney V., Yachie A., Szabo R.P., Wagner O., Vercellotti G.M., Eaton J.W., Balla G., Balla J. Oxidation of hemoglobin by lipid hydroperoxide associated with low-density lipoprotein (LDL) and increased cytotoxic effect by LDL oxidation in heme oxygenase-1 (HO-1) deficiency. Cell Mol. Biol. 2005, 51:377-385.
    • (2005) Cell Mol. Biol. , vol.51 , pp. 377-385
    • Nagy, E.1    Jeney, V.2    Yachie, A.3    Szabo, R.P.4    Wagner, O.5    Vercellotti, G.M.6    Eaton, J.W.7    Balla, G.8    Balla, J.9
  • 66
    • 0003303966 scopus 로고
    • Quantitative determination of myoglobin and haemoglobin in beef by high-performance liquid chromatography
    • Oellingrath I.M., Iverson A., Skreds G. Quantitative determination of myoglobin and haemoglobin in beef by high-performance liquid chromatography. Meat Sci. 1990, 28:313-320.
    • (1990) Meat Sci. , vol.28 , pp. 313-320
    • Oellingrath, I.M.1    Iverson, A.2    Skreds, G.3
  • 67
    • 4644371601 scopus 로고
    • Influences of heme pigment, non-heme iron, and nitrite on lipid oxidation in cooked mackerel meat
    • Ohshima T., Wada S., Koizumi C. Influences of heme pigment, non-heme iron, and nitrite on lipid oxidation in cooked mackerel meat. Nippon Suisan Gakkaishi 1988, 54:2165-2171.
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 2165-2171
    • Ohshima, T.1    Wada, S.2    Koizumi, C.3
  • 68
    • 0030773396 scopus 로고    scopus 로고
    • 2, NO, and CO by electrostatic interactions with the bound ligand
    • 2, NO, and CO by electrostatic interactions with the bound ligand. J. Biol. Inorg. Chem. 1997, 2:544-552.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 544-552
    • Olson, J.S.1    Phillips, G.N.2
  • 70
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains
    • Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A., Baker E.N. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains. Nat. Struct. Biol. 1999, 6:926-931.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 71
    • 33745757012 scopus 로고    scopus 로고
    • Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems
    • Park D., Xiong Y.L., Alderton A.L., Ooizumi T. Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems. J. Agric. Food Chem. 2006, 54:4445-4451.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 4445-4451
    • Park, D.1    Xiong, Y.L.2    Alderton, A.L.3    Ooizumi, T.4
  • 73
    • 7244241582 scopus 로고
    • Separation of meat pigment by gel filtration on sephadex
    • Pisula A. Separation of meat pigment by gel filtration on sephadex. Zeszyty Problemowe Postfpow Nauk Rolniczych 1975, 167:115-118.
    • (1975) Zeszyty Problemowe Postfpow Nauk Rolniczych , vol.167 , pp. 115-118
    • Pisula, A.1
  • 74
    • 0002261351 scopus 로고
    • The effects of exsanguination of sockeye salmon on the changes of lipid composition during frozen storage
    • Fishing News Books, Oxford, E.G. Bligh (Ed.)
    • Porter P.J., Kennish J.M., Kramer D.E. The effects of exsanguination of sockeye salmon on the changes of lipid composition during frozen storage. Seafood Science and Technology 1992, Fishing News Books, Oxford. E.G. Bligh (Ed.).
    • (1992) Seafood Science and Technology
    • Porter, P.J.1    Kennish, J.M.2    Kramer, D.E.3
  • 75
    • 3242746585 scopus 로고    scopus 로고
    • Regio- and stereo-chemical oxidation of linoleic acid by human myoglobin and hydrogen peroxide: Tyr(103) affects rate and product distribution
    • Rayner B.S., Stocker R., Lay P.A., Witting P.K. Regio- and stereo-chemical oxidation of linoleic acid by human myoglobin and hydrogen peroxide: Tyr(103) affects rate and product distribution. Biochem. J. 2004, 381:365-372.
    • (2004) Biochem. J. , vol.381 , pp. 365-372
    • Rayner, B.S.1    Stocker, R.2    Lay, P.A.3    Witting, P.K.4
  • 76
    • 0037039353 scopus 로고    scopus 로고
    • Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin
    • Reeder B.J., Svistunenko D.A., Sharpe M.S., Wilson M.T. Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin. Biochemistry 2002, 41:367-375.
    • (2002) Biochemistry , vol.41 , pp. 367-375
    • Reeder, B.J.1    Svistunenko, D.A.2    Sharpe, M.S.3    Wilson, M.T.4
  • 77
    • 7244243910 scopus 로고    scopus 로고
    • The radical and redox chemistry of myoglobin and hemoglobfrom in vitro studies to human pathology
    • Reeder B.J., Svistunenko D.A., Cooper C.E., Wilson M.T. The radical and redox chemistry of myoglobin and hemoglobfrom in vitro studies to human pathology. Antioxid Redox Signal 2004, 6:954-966.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 954-966
    • Reeder, B.J.1    Svistunenko, D.A.2    Cooper, C.E.3    Wilson, M.T.4
  • 79
    • 0002467388 scopus 로고
    • Lipid oxidation in retail beef, pork and chicken muscles as affected by concentrations of heme pigments and nonheme iron and microsomal enzymic lipid peroxidation activity
    • Rhee K.S., Ziprin Y.A. Lipid oxidation in retail beef, pork and chicken muscles as affected by concentrations of heme pigments and nonheme iron and microsomal enzymic lipid peroxidation activity. J. Food Biochem. 1987, 11:1-15.
    • (1987) J. Food Biochem. , vol.11 , pp. 1-15
    • Rhee, K.S.1    Ziprin, Y.A.2
  • 80
    • 0038115411 scopus 로고    scopus 로고
    • Comparative analysis of different hemoglobins: autoxidation, reaction with peroxide, and lipid oxidation
    • Richards M.P., Dettmann M.A. Comparative analysis of different hemoglobins: autoxidation, reaction with peroxide, and lipid oxidation. J. Agric. Food Chem. 2003, 51:3886-3891.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 3886-3891
    • Richards, M.P.1    Dettmann, M.A.2
  • 81
    • 0037196137 scopus 로고    scopus 로고
    • Contributions of blood and blood components to lipid oxidation in fish muscle
    • Richards M.P., Hultin H.O. Contributions of blood and blood components to lipid oxidation in fish muscle. J. Agric. Food Chem. 2002, 50:555-564.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 555-564
    • Richards, M.P.1    Hultin, H.O.2
  • 82
    • 0035997454 scopus 로고    scopus 로고
    • Role of deoxyhemoglobin in lipid oxidation of washed cod muscle mediated by trout, poultry and beef hemoglobins
    • Richards M.P., Modra A.M., Li R. Role of deoxyhemoglobin in lipid oxidation of washed cod muscle mediated by trout, poultry and beef hemoglobins. Meat Sci. 2002, 62:157-163.
    • (2002) Meat Sci. , vol.62 , pp. 157-163
    • Richards, M.P.1    Modra, A.M.2    Li, R.3
  • 83
    • 30544443689 scopus 로고    scopus 로고
    • Pro-oxidative characteristics of trout hemoglobin and myoglobA role for released heme in oxidation of lipids
    • Richards M.P., Dettmann M.A., Grunwald E.W. Pro-oxidative characteristics of trout hemoglobin and myoglobA role for released heme in oxidation of lipids. J. Agric. Food Chem. 2005, 53:10231-10238.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 10231-10238
    • Richards, M.P.1    Dettmann, M.A.2    Grunwald, E.W.3
  • 84
    • 34249304823 scopus 로고    scopus 로고
    • Effects of fish heme protein structure and lipid substrate composition on hemoglobin-mediated lipid oxidation
    • Richards M.P., Nelson N.M., Kristinsson H.G., Mony S.S., Petty H.T., Oliveira A.C. Effects of fish heme protein structure and lipid substrate composition on hemoglobin-mediated lipid oxidation. J. Agric. Food Chem. 2007, 55:3643-3654.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 3643-3654
    • Richards, M.P.1    Nelson, N.M.2    Kristinsson, H.G.3    Mony, S.S.4    Petty, H.T.5    Oliveira, A.C.6
  • 85
    • 77951452615 scopus 로고    scopus 로고
    • Effect of pH on structural changes in perch hemoglobin that can alter redox stability and heme affinity
    • Richards M.P., Aranda IVR., Cai H., Phillips G.N. Effect of pH on structural changes in perch hemoglobin that can alter redox stability and heme affinity. J. Aquatic Food Product Technol. 2009, 18:416-423.
    • (2009) J. Aquatic Food Product Technol. , vol.18 , pp. 416-423
    • Richards, M.P.1    Aranda, I.V.R.2    Cai, H.3    Phillips, G.N.4
  • 86
    • 0033428049 scopus 로고    scopus 로고
    • Fish hemoglobins: the order Clupeiformes
    • Rizzotti M., Gioppato F. Fish hemoglobins: the order Clupeiformes. Rev. Fish Biol. Fish. 1999, 9:71-87.
    • (1999) Rev. Fish Biol. Fish. , vol.9 , pp. 71-87
    • Rizzotti, M.1    Gioppato, F.2
  • 87
    • 84987355447 scopus 로고
    • Warmed-over flavor in cooked meats
    • Sato K., Hegarty G.R. Warmed-over flavor in cooked meats. J. Food Sci. 1971, 36:1098-1102.
    • (1971) J. Food Sci. , vol.36 , pp. 1098-1102
    • Sato, K.1    Hegarty, G.R.2
  • 89
    • 5744250269 scopus 로고    scopus 로고
    • Comparison of a natural rosemary extract and BHA/BHT for relative antioxidant effectiveness in pork sausage
    • Sebranek J.G., Sewaltc V.J.H., K.L R., Houser T.A. Comparison of a natural rosemary extract and BHA/BHT for relative antioxidant effectiveness in pork sausage. Meat Sci. 2005, 69:289-296.
    • (2005) Meat Sci. , vol.69 , pp. 289-296
    • Sebranek, J.G.1    Sewaltc, V.J.H.2    Houser, T.A.3
  • 90
    • 10944271892 scopus 로고    scopus 로고
    • Internal premature browning in cooked ground beef patties from high-oxygen modified atmosphere packaging
    • Seyfert M., Mancini R.A., Hunt M.C. Internal premature browning in cooked ground beef patties from high-oxygen modified atmosphere packaging. J. Food Sci. 2004, 69:721-725.
    • (2004) J. Food Sci. , vol.69 , pp. 721-725
    • Seyfert, M.1    Mancini, R.A.2    Hunt, M.C.3
  • 91
    • 0001023291 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for myoglobin and hemogloba venerable puzzle
    • Shikama K. The molecular mechanism of autoxidation for myoglobin and hemogloba venerable puzzle. Chem. Rev. 1998, 98:1357-1373.
    • (1998) Chem. Rev. , vol.98 , pp. 1357-1373
    • Shikama, K.1
  • 92
    • 0000208426 scopus 로고
    • Surimi from dark fleshed species
    • Marcel Dekker, New York, T.C. Lanier, C.M. Lee (Eds.)
    • Shimizu Y., Toyohara H., Lanier T.C. Surimi from dark fleshed species. Surimi Technology 1992, Marcel Dekker, New York. T.C. Lanier, C.M. Lee (Eds.).
    • (1992) Surimi Technology
    • Shimizu, Y.1    Toyohara, H.2    Lanier, T.C.3
  • 94
    • 28444435504 scopus 로고    scopus 로고
    • The relation of lipid peroxidation processes with atherogenesis: a new theory on atherogenesis
    • Spiteller G. The relation of lipid peroxidation processes with atherogenesis: a new theory on atherogenesis. Mol. Nutr. Food Res. 2005, 49:999-1013.
    • (2005) Mol. Nutr. Food Res. , vol.49 , pp. 999-1013
    • Spiteller, G.1
  • 95
    • 66149131355 scopus 로고    scopus 로고
    • Dietary nitrite prevents hypercholesterolemic microvascular inflammation and reverses endothelial dysfunction
    • Stokes K.Y., Dugas T.R., Tang Y., Garg H., Guidry E., Bryan N.S. Dietary nitrite prevents hypercholesterolemic microvascular inflammation and reverses endothelial dysfunction. Am. J. Physiol. Heart Circ. Physiol. 2009, 296:1281-1288.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296 , pp. 1281-1288
    • Stokes, K.Y.1    Dugas, T.R.2    Tang, Y.3    Garg, H.4    Guidry, E.5    Bryan, N.S.6
  • 96
    • 0037448110 scopus 로고    scopus 로고
    • Ascorbate does not act as a pro-oxidant towards lipids and proteins in human plasma exposed to redox-active transition metal ions and hydrogen peroxide
    • Suh J., Zhu B.Z., Frei B. Ascorbate does not act as a pro-oxidant towards lipids and proteins in human plasma exposed to redox-active transition metal ions and hydrogen peroxide. Free Radic. Biol. Med. 2003, 34:1306-1314.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1306-1314
    • Suh, J.1    Zhu, B.Z.2    Frei, B.3
  • 97
    • 33744473116 scopus 로고    scopus 로고
    • Redox instability induced by 4-hydroxy-2-nonenal in porcine and bovine myoglobins at pH 5.6 and 4 degrees C
    • Suman S.P., Faustman C., Stamer S.L., Liebler D.C. Redox instability induced by 4-hydroxy-2-nonenal in porcine and bovine myoglobins at pH 5.6 and 4 degrees C. J. Agric. Food Chem. 2006, 54:3402-3408.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 3402-3408
    • Suman, S.P.1    Faustman, C.2    Stamer, S.L.3    Liebler, D.C.4
  • 98
    • 0028337141 scopus 로고
    • Mechanism of the biphasic effect of ethylenediaminetetraacetate on lipid peroxidation in iron-supported and reconstituted enzymatic system
    • Tampo Y., Onodera S., Yonaha M. Mechanism of the biphasic effect of ethylenediaminetetraacetate on lipid peroxidation in iron-supported and reconstituted enzymatic system. Free Radic. Biol. Med. 1994, 17:27-34.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 27-34
    • Tampo, Y.1    Onodera, S.2    Yonaha, M.3
  • 99
    • 0032510761 scopus 로고    scopus 로고
    • Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin
    • Tang Q., Kalsbeck W.A., Olson J.S., Bocian D.F. Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin. Biochemistry 1998, 37:7047-7056.
    • (1998) Biochemistry , vol.37 , pp. 7047-7056
    • Tang, Q.1    Kalsbeck, W.A.2    Olson, J.S.3    Bocian, D.F.4
  • 100
    • 0001133973 scopus 로고
    • Unsaturated lipid oxidation catalyzed by hematin compounds
    • Tappel A.L. Unsaturated lipid oxidation catalyzed by hematin compounds. J. Biol. Chem. 1955, 217:721-733.
    • (1955) J. Biol. Chem. , vol.217 , pp. 721-733
    • Tappel, A.L.1
  • 101
    • 0000837366 scopus 로고
    • The rate of metmyoglobin formation in beef, pork, and turkey meat as influenced by pH, sodium chloride, and sodium tripolyphosphate
    • Trout G.R. The rate of metmyoglobin formation in beef, pork, and turkey meat as influenced by pH, sodium chloride, and sodium tripolyphosphate. Meat Sci. 1990, 28:203-210.
    • (1990) Meat Sci. , vol.28 , pp. 203-210
    • Trout, G.R.1
  • 102
    • 0038746781 scopus 로고    scopus 로고
    • Aqueous extracts from some muscles inhibit hemoglobin-mediated oxidation of cod muscle membrane lipids
    • Undeland I., Hultin H.O., Richards M.P. Aqueous extracts from some muscles inhibit hemoglobin-mediated oxidation of cod muscle membrane lipids. J. Agric. Food Chem. 2003, 51:3111-3119.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 3111-3119
    • Undeland, I.1    Hultin, H.O.2    Richards, M.P.3
  • 103
    • 0030031737 scopus 로고    scopus 로고
    • ESR spin trapping investigation of radical formation from the reaction between hematin and tert-butyl hydroperoxide
    • Van Der Zee J., Barr D.P., Mason R.P. ESR spin trapping investigation of radical formation from the reaction between hematin and tert-butyl hydroperoxide. Free Radic. Biol. Med. 1996, 20:199-206.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 199-206
    • Van Der Zee, J.1    Barr, D.P.2    Mason, R.P.3
  • 104
    • 0034708352 scopus 로고    scopus 로고
    • Enhanced lipid oxidation by oxidatively modified myoglobrole of protein-bound heme
    • Vuletich J.L., Osawa Y., Aviram M. Enhanced lipid oxidation by oxidatively modified myoglobrole of protein-bound heme. Biochem. Biophys. Res. Commun. 2000, 269:647-651.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 647-651
    • Vuletich, J.L.1    Osawa, Y.2    Aviram, M.3
  • 105
    • 0025599818 scopus 로고
    • Nitrates, nitrites and N-nitrosocompounds: a review of the occurrence in food and diet and the toxicological implications
    • Walker R. Nitrates, nitrites and N-nitrosocompounds: a review of the occurrence in food and diet and the toxicological implications. Food Aditt. Contam. 1990, 7:717-768.
    • (1990) Food Aditt. Contam. , vol.7 , pp. 717-768
    • Walker, R.1
  • 106
    • 84986870335 scopus 로고
    • The residual blood content of meat - a review
    • Warriss P.D. The residual blood content of meat - a review. J. Sci. Food Agric. 1977, 28:457-462.
    • (1977) J. Sci. Food Agric. , vol.28 , pp. 457-462
    • Warriss, P.D.1
  • 107
    • 0026701964 scopus 로고
    • Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation
    • Wazawa T., Matsuoka A., Tajima G., Sugawara Y., Nakamura K., Shikama K. Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation. Biophys. J. 1992, 63:544-550.
    • (1992) Biophys. J. , vol.63 , pp. 544-550
    • Wazawa, T.1    Matsuoka, A.2    Tajima, G.3    Sugawara, Y.4    Nakamura, K.5    Shikama, K.6
  • 108
    • 0020045904 scopus 로고
    • Neutrophil-mediated methemoglobin formation in the erythrocyte
    • Weiss S.J. Neutrophil-mediated methemoglobin formation in the erythrocyte. J. Biol. Chem. 1982, 257:2947-2953.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2947-2953
    • Weiss, S.J.1
  • 109
    • 0023654845 scopus 로고
    • Temperature adaptation of fish hemoglobins reflected in rates of autoxidation
    • Wilson R.R.J., Knowles F. Temperature adaptation of fish hemoglobins reflected in rates of autoxidation. Arch. Biochem. Biophys. 1987, 255:210-213.
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 210-213
    • Wilson, R.R.J.1    Knowles, F.2
  • 110
    • 0037167618 scopus 로고    scopus 로고
    • Role of tyrosine-103 in myoglobin peroxidase activity: kinetic and steady-state studies on the reaction of wild-type and variant recombinant human myoglobins with H(2)O(2)
    • Witting P.K., Mauk A.G., Lay P.A. Role of tyrosine-103 in myoglobin peroxidase activity: kinetic and steady-state studies on the reaction of wild-type and variant recombinant human myoglobins with H(2)O(2). Biochemistry 2002, 41:11495-11503.
    • (2002) Biochemistry , vol.41 , pp. 11495-11503
    • Witting, P.K.1    Mauk, A.G.2    Lay, P.A.3
  • 111
    • 0347650813 scopus 로고
    • Lack of changes in fatty acid composition of mackerel and cod during iced and frozen storage
    • Xing Y., Yoo Y., Kelleher S.D., Nawar W.W., Hultin H.O. Lack of changes in fatty acid composition of mackerel and cod during iced and frozen storage. J. Food Lipids 1993, 1:1-14.
    • (1993) J. Food Lipids , vol.1 , pp. 1-14
    • Xing, Y.1    Yoo, Y.2    Kelleher, S.D.3    Nawar, W.W.4    Hultin, H.O.5
  • 112
    • 0000780698 scopus 로고
    • Influence of temperature, pH, and phospholipid composition upon the stability of myoglobin and phospholipid: a liposomal model
    • Yin M.-C., Faustman C. Influence of temperature, pH, and phospholipid composition upon the stability of myoglobin and phospholipid: a liposomal model. J. Agric. Food Chem. 1993, 41:853-857.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 853-857
    • Yin, M.-C.1    Faustman, C.2
  • 113
    • 0023661090 scopus 로고
    • Oxidation of oxymyoglobin to metmyoglobin with hydrogen peroxide: involvement of ferryl intermediate
    • Yusa K., Shikama K. Oxidation of oxymyoglobin to metmyoglobin with hydrogen peroxide: involvement of ferryl intermediate. Biochemistry 1987, 26:6684-6688.
    • (1987) Biochemistry , vol.26 , pp. 6684-6688
    • Yusa, K.1    Shikama, K.2


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