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2003 | 08 | 2 |

Tytuł artykułu

The influence of metmyoglobin and ferrylmyoglobin on the human erythrocyte membrane

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Preliminary experiments revealed that ferrylmyoglobin decayed more slowly in the absence than in the presence of intact erythrocytes and erythrocyte membranes. This suggested the existence of interactions between FerrylMb and the erythrocyte membrane. Subsequent studies examined the influence of FerrylMb on the membrane of intact erythrocytes and on isolated erythrocyte membranes. The incubation of intact erythrocytes with FerrylMb did not influence their osmotic fragility or the fluidity of their membranes; the level of peroxidation of the membrane lipids increased only slightly (there was only a slight increase in the level of membrane lipid peroxidation). The activity of acetylcholinesterase significantly increased after 15 minutes of incubation, whereas longer incubation did not lead to any changes in the activity of this enzyme. The incubation of isolated erythrocyte membranes with FerrylMb resulted in an increase in their fluidity and a significant rise in the level of lipid peroxidation.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

08

Numer

2

Opis fizyczny

p.337-342,fig.

Twórcy

autor
  • University of Lodz, Banacha 12-16, 90-237 Lodz, Poland
autor

Bibliografia

  • 1.Irwin, J.A., Østdal, H. and Davies, M.J. Myoglobin - induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. Arch. Biochem. Biophys. 362 (1999) 94-104.
  • 2.Carlsen, C.U., Maiken, V., Kröger-Ohlsen, M.V., Bellio, R. and Skibsted, L.H. Protein binding in deactivation of ferrylmyoglobin by chlorogenate and ascorbate. J. Agr. Food Chem. 48 (2000) 204-212.
  • 3.Østdal, H., Søgaard, S.G., Bendixen, E. and Andersen, H.J. Protein radicals in the reaction between H202-activated metmyoglobin and bovine serum albumin. Free Radical Res. 35 (2001) 757-766.
  • 4.Baron, C.P., Skibsted, L.H. and Andersen, H.J. Peroxidation of linoleate at physiological pH: Hemichrome formation by substrate binding protect against metmyoglobin activation by hydrogen peroxide. Free Radical Biol. Med. 28 (2000) 549-558.
  • 5.Baron, C.P., Skibsted, L.H. and Andersen, H.J. Concentration effects in myoglobin-catalyzed peroxidation of linoleate. J. Agr. Food Chem. 50 (2002) 883-888.
  • 6.Vuletich, J.L., Osawa, Y. and Aviram, M. Enhanced lipid oxidation by oxidatively modified myoglobin: Role of protein-bound heme. Biochem. Biophys. Res. Comm. 269 (2000) 647-651.
  • 7.Ortiz de Montellano, P.R. and Catalano, C.E. Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxidizing equivalents to the protein surface. J. Biol. Chem. 260 (1985) 9265-9271.
  • 8.Miura, T., Muraoka, S. and Ogiso, T. Relationship between protein damage and ferrylmyoglobin. Biochem. Mol. Biol. Int. 36 (1995) 587-594.
  • 9.Østdal, H., Andersen, H.J. and Davies, M.J. Formation of long-lived radicals on proteins by radical transfer from heme enzymes - A common process? Arch. Biochem. Biophys. (1999) 105-113.
  • 10.Dodge, J.T., Mitchell, C. and Hanahan, I. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 100 (1963) 119-130.
  • 11.Ellman, G.L., Courtney, K.D., Anders, V. et al. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7 (1961) 88-95.
  • 12.Stocks, J. and Dromandy, T.L. The autooxidation of human red cell lipids induced by hydrogen peroxide. Br. J. Haematol. 20 (1971) 95-111.
  • 13.Van der Meer, B.W. Subcellular Biochemistry. Fluorescence Studies on Biological Membranes (Hilderson, H.J. and Harris, J.R. Eds.). Plenum Press. New York 13 (1988) 1-53.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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