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Volumn 123, Issue 2, 2010, Pages 231-236

Catalytic mechanisms of metmyoglobin on the oxidation of lipids in phospholipid liposome model system

Author keywords

Iron chelating agents; Lipid oxidation; Liposome system; Metmyoglobin

Indexed keywords

DEFEROXAMINE; FERRIC ION; LIPOSOME; METMYOGLOBIN; PENTETIC ACID;

EID: 77953288299     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2010.04.013     Document Type: Article
Times cited : (16)

References (39)
  • 1
    • 0031992541 scopus 로고    scopus 로고
    • Prooxidant effects of ferrous iron, hemoglobin, and ferritin in oil emulsion and cooked meat homogenates are different from those in raw-meat homogenates
    • Ahn D.U., and Kim S.M. Prooxidant effects of ferrous iron, hemoglobin, and ferritin in oil emulsion and cooked meat homogenates are different from those in raw-meat homogenates. Poultry Science 77 (1998) 348-355
    • (1998) Poultry Science , vol.77 , pp. 348-355
    • Ahn, D.U.1    Kim, S.M.2
  • 2
    • 84986528169 scopus 로고
    • Dietary α-linolenic acid and mixed tocopherols, and packaging influences on lipid stability in broiler chicken breast and leg muscle
    • Ahn D.U., Wolfe F.H., and Sim J.S. Dietary α-linolenic acid and mixed tocopherols, and packaging influences on lipid stability in broiler chicken breast and leg muscle. Journal of Food Science 60 (1995) 1013-1018
    • (1995) Journal of Food Science , vol.60 , pp. 1013-1018
    • Ahn, D.U.1    Wolfe, F.H.2    Sim, J.S.3
  • 7
    • 0029947826 scopus 로고    scopus 로고
    • Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: Possibly related to the rates of hemin release
    • Chiu D.T., van den Berg J., Kuypers F.A., Hung I., Wei J., and Liu T. Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: Possibly related to the rates of hemin release. Free Radical Biology and Medicine 21 (1996) 89-95
    • (1996) Free Radical Biology and Medicine , vol.21 , pp. 89-95
    • Chiu, D.T.1    van den Berg, J.2    Kuypers, F.A.3    Hung, I.4    Wei, J.5    Liu, T.6
  • 8
    • 0025652977 scopus 로고
    • Detection of myoglobin-derived radicals on reaction of metmyoglobin with hydrogen peroxide and other peroxidic compounds
    • Davies M.J. Detection of myoglobin-derived radicals on reaction of metmyoglobin with hydrogen peroxide and other peroxidic compounds. Free Radical Research and Communications 10 (1990) 361-370
    • (1990) Free Radical Research and Communications , vol.10 , pp. 361-370
    • Davies, M.J.1
  • 9
    • 0021842958 scopus 로고
    • Conversion of linoleic acid hydroperoxide to hydroxyl, keto, epoxyhydroxy, and trihydroxy fatty acids by hematin
    • Dix T.A., and Marnett L.J. Conversion of linoleic acid hydroperoxide to hydroxyl, keto, epoxyhydroxy, and trihydroxy fatty acids by hematin. The Journal of Biological Chemistry 260 (1985) 5351-5357
    • (1985) The Journal of Biological Chemistry , vol.260 , pp. 5351-5357
    • Dix, T.A.1    Marnett, L.J.2
  • 10
    • 0034634543 scopus 로고    scopus 로고
    • Formation of compound I in the reaction of native myoglobins with hydrogen peroxide
    • Egawa T., Shimada H., and Ishimura Y. Formation of compound I in the reaction of native myoglobins with hydrogen peroxide. Journal of Biological Chemistry 275 (2000) 34858-34866
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 34858-34866
    • Egawa, T.1    Shimada, H.2    Ishimura, Y.3
  • 11
    • 0023371167 scopus 로고
    • Secondary products of lipid peroxidation
    • Frankel E.N. Secondary products of lipid peroxidation. Chemistry and Physics in Lipids 44 (1987) 73-85
    • (1987) Chemistry and Physics in Lipids , vol.44 , pp. 73-85
    • Frankel, E.N.1
  • 12
    • 0000683151 scopus 로고    scopus 로고
    • Lipoxygenase activity in pig muscle: Purification and partial characterization
    • Gata J.L., Pinto M.C., and Macias P. Lipoxygenase activity in pig muscle: Purification and partial characterization. Journal of Agricultural and Food Chemistry 44 (1996) 2573-2577
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 2573-2577
    • Gata, J.L.1    Pinto, M.C.2    Macias, P.3
  • 13
    • 0035543050 scopus 로고    scopus 로고
    • Oxymyoglobin oxidation and membranal lipid peroxidation initiated by iron redox cycle
    • Gorelik S., and Kanner J. Oxymyoglobin oxidation and membranal lipid peroxidation initiated by iron redox cycle. Journal of Agricultural and Food Chemistry 49 (2001) 5939-5944
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 5939-5944
    • Gorelik, S.1    Kanner, J.2
  • 15
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B., and Gutteridge J.M.C. Role of free radicals and catalytic metal ions in human disease: An overview. Methods in Enzymology 186 (1990) 1-85
    • (1990) Methods in Enzymology , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 16
    • 0023693165 scopus 로고
    • The generation of ferryl or hydroxyl radicals during interaction of haemproteins with hydrogen peroxide
    • Harel S., and Kanner J. The generation of ferryl or hydroxyl radicals during interaction of haemproteins with hydrogen peroxide. Free Radical Research and Communications 5 (1988) 21-33
    • (1988) Free Radical Research and Communications , vol.5 , pp. 21-33
    • Harel, S.1    Kanner, J.2
  • 17
    • 0024551688 scopus 로고
    • Haemoglobin and myoglobin as inhibitors of hydroxyl radical generation in a model system of "iron redox" cycle
    • Harel S., and Kanner J. Haemoglobin and myoglobin as inhibitors of hydroxyl radical generation in a model system of "iron redox" cycle. Free Radical Research and Communications 1 (1989) 1-10
    • (1989) Free Radical Research and Communications , vol.1 , pp. 1-10
    • Harel, S.1    Kanner, J.2
  • 18
    • 0024269252 scopus 로고
    • Iron release from metmyoglobin methaemoglobin and cytochrome c by a system generating hydrogen peroxide
    • Harel S., Salan M.A., and Kanner J. Iron release from metmyoglobin methaemoglobin and cytochrome c by a system generating hydrogen peroxide. Free Radical Research and Communications 5 (1988) 11-19
    • (1988) Free Radical Research and Communications , vol.5 , pp. 11-19
    • Harel, S.1    Salan, M.A.2    Kanner, J.3
  • 19
    • 0022001719 scopus 로고
    • Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin
    • Kanner J., and Harel S. Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Archives of Biochemistry and Biophysics 237 (1985) 314-321
    • (1985) Archives of Biochemistry and Biophysics , vol.237 , pp. 314-321
    • Kanner, J.1    Harel, S.2
  • 23
    • 0016713756 scopus 로고
    • Lipid oxidation in biological membranes. Electron transfer proteins as initiators of lipid autoxidation
    • Kaschnitz R.M., and Hatefi Y. Lipid oxidation in biological membranes. Electron transfer proteins as initiators of lipid autoxidation. Archives of Biochemistry and Biophysics 171 (1975) 292-304
    • (1975) Archives of Biochemistry and Biophysics , vol.171 , pp. 292-304
    • Kaschnitz, R.M.1    Hatefi, Y.2
  • 24
    • 0025880282 scopus 로고
    • Hematin- and peroxide-catalyzed peroxidation of phospholipid liposomes
    • Kim E.J., and Sevanian A. Hematin- and peroxide-catalyzed peroxidation of phospholipid liposomes. Archives of Biochemistry and Biophysics 288 (1991) 324-330
    • (1991) Archives of Biochemistry and Biophysics , vol.288 , pp. 324-330
    • Kim, E.J.1    Sevanian, A.2
  • 25
    • 0001924192 scopus 로고
    • The determination of haem pigments in meat
    • Krzywicki K. The determination of haem pigments in meat. Meat Science 7 (1982) 29-36
    • (1982) Meat Science , vol.7 , pp. 29-36
    • Krzywicki, K.1
  • 27
    • 19944412184 scopus 로고    scopus 로고
    • Lipid hydroperoxidase activity of myoglobin and phenolic antioxidants in simulated gastric fluid
    • Lapidot T., Granit R., and Kanner J. Lipid hydroperoxidase activity of myoglobin and phenolic antioxidants in simulated gastric fluid. Journal of Agricultural and Food Chemistry 53 (2005) 3391-3396
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 3391-3396
    • Lapidot, T.1    Granit, R.2    Kanner, J.3
  • 28
    • 33846154149 scopus 로고    scopus 로고
    • Mechanism of lipid peroxidation in meat and meat products - A review
    • Min B., and Ahn D.U. Mechanism of lipid peroxidation in meat and meat products - A review. Food Science and Biotechnology 14 (2005) 152-163
    • (2005) Food Science and Biotechnology , vol.14 , pp. 152-163
    • Min, B.1    Ahn, D.U.2
  • 29
    • 58649102225 scopus 로고    scopus 로고
    • Factors in various fractions of meat homogenates that affect the oxidative stability of raw chicken breast and beef loin
    • Min B., and Ahn D.U. Factors in various fractions of meat homogenates that affect the oxidative stability of raw chicken breast and beef loin. Journal of Food Science 74 (2009) C41-48
    • (2009) Journal of Food Science , vol.74
    • Min, B.1    Ahn, D.U.2
  • 30
    • 0024461666 scopus 로고
    • Effects of oxyradicals on oxymyoglobin. Deoxygenation, haem removal and iron release
    • Prasad M.R., Engelman R.M., Jones R.M., and Das D.K. Effects of oxyradicals on oxymyoglobin. Deoxygenation, haem removal and iron release. Biochemical Journal 263 (1989) 731-736
    • (1989) Biochemical Journal , vol.263 , pp. 731-736
    • Prasad, M.R.1    Engelman, R.M.2    Jones, R.M.3    Das, D.K.4
  • 31
    • 0023897833 scopus 로고
    • Formation of hydroxyl radicals in biological systems. Does myoglobin stimulate hydroxyl radical formation from hydrogen peroxide?
    • Puppo A., and Halliwell B. Formation of hydroxyl radicals in biological systems. Does myoglobin stimulate hydroxyl radical formation from hydrogen peroxide?. Free Radical Research and Communications 4 (1988) 415-422
    • (1988) Free Radical Research and Communications , vol.4 , pp. 415-422
    • Puppo, A.1    Halliwell, B.2
  • 33
    • 0024311315 scopus 로고
    • Reaction of hydroxyl radicals with the ferrous and ferric iron chelates of diethylenetriamine-N, N, N', N", N"-pentaacetate
    • Rahhal S., and Richter H.W. Reaction of hydroxyl radicals with the ferrous and ferric iron chelates of diethylenetriamine-N, N, N', N", N"-pentaacetate. Free Radical Research and Communications 6 (1989) 369-377
    • (1989) Free Radical Research and Communications , vol.6 , pp. 369-377
    • Rahhal, S.1    Richter, H.W.2
  • 34
    • 0028174937 scopus 로고
    • The lipoxygenase activity of myoglobin. Oxidation of linoleic acid by the ferryl oxygen rather than protein radical
    • Rao S.I., Wilks A., Hamberg M., and Ortiz de Montellano P.R. The lipoxygenase activity of myoglobin. Oxidation of linoleic acid by the ferryl oxygen rather than protein radical. The Journal of Biological Chemistry 269 (1994) 7210-7216
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 7210-7216
    • Rao, S.I.1    Wilks, A.2    Hamberg, M.3    Ortiz de Montellano, P.R.4
  • 35
    • 0032521652 scopus 로고    scopus 로고
    • Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid
    • Reeder B.J., and Wilson M.T. Mechanism of reaction of myoglobin with the lipid hydroperoxide hydroperoxyoctadecadienoic acid. Biochemical Journal 330 (1998) 1317-1323
    • (1998) Biochemical Journal , vol.330 , pp. 1317-1323
    • Reeder, B.J.1    Wilson, M.T.2
  • 36
    • 0035371323 scopus 로고    scopus 로고
    • The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species
    • Reeder B.J., and Wilson M.T. The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species. Free Radical Biology and Medicine 30 (2001) 1311-1318
    • (2001) Free Radical Biology and Medicine , vol.30 , pp. 1311-1318
    • Reeder, B.J.1    Wilson, M.T.2
  • 38
    • 0024431857 scopus 로고
    • The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine
    • Rice-Evans C., Okunade G., and Khan R. The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine. Free Radical Research and Communications 7 (1989) 45-54
    • (1989) Free Radical Research and Communications , vol.7 , pp. 45-54
    • Rice-Evans, C.1    Okunade, G.2    Khan, R.3
  • 39
    • 0027359301 scopus 로고
    • Hemin-induced lipid membrane disorder and increased permeability: A molecular model for the mechanism of cell lysis
    • Schmitt T.H., Frezzatti W.A., and Schreier S. Hemin-induced lipid membrane disorder and increased permeability: A molecular model for the mechanism of cell lysis. Archives of Biochemistry and Biophysics 307 (1993) 96-103
    • (1993) Archives of Biochemistry and Biophysics , vol.307 , pp. 96-103
    • Schmitt, T.H.1    Frezzatti, W.A.2    Schreier, S.3


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