메뉴 건너뛰기




Volumn 31, Issue 3, 1999, Pages 201-210

Decrease in 2,2,6,6-tetramethyl-piperidine-1-oxyl (TEMPO) EPR signal in ozone-treated erythrocyte membranes

Author keywords

Electron paramagnetic resonance; Erythrocyte membrane; Nitroxide radical; Oxidative stress; Ozone

Indexed keywords

LIPID; NITROXIDE; OZONE; PROTEIN; RADICAL; TEMPOL; UNSATURATED FATTY ACID;

EID: 0042219603     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715769900300761     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0023158539 scopus 로고
    • Toxicity and biochemical mechanisms of ozone
    • MA. Mehlman and C. Borek (1987) Toxicity and biochemical mechanisms of ozone. Environmental Research, 42, 36-53.
    • (1987) Environmental Research , vol.42 , pp. 36-53
    • Mehlman, M.A.1    Borek, C.2
  • 2
    • 0028080284 scopus 로고
    • Mechanisms of radical formation from reactions of ozone with target molecules in the lung
    • W.A. Pryor (1994) Mechanisms of radical formation from reactions of ozone with target molecules in the lung. Free Radicals in Biology and Medicine, 17, 451-465.
    • (1994) Free Radicals in Biology and Medicine , vol.17 , pp. 451-465
    • Pryor, W.A.1
  • 3
    • 0028840467 scopus 로고
    • The cascade mechanism to explain ozone toxicity: The role of lipid ozonation products
    • W.A. Pryor, G.L. Squadrito and M. Friedman (1995) The cascade mechanism to explain ozone toxicity: the role of lipid ozonation products. Free Radicals in Biology and Medicine, 19, 935-941.
    • (1995) Free Radicals in Biology and Medicine , vol.19 , pp. 935-941
    • Pryor, W.A.1    Squadrito, G.L.2    Friedman, M.3
  • 4
    • 0345378413 scopus 로고
    • Free radical production from the ozonation of simple alkenes, fatty acid emulsions and phosphatidylcholine liposomes
    • (Ed. K.J.A. Davies), Pergamon Press, Oxford
    • D.F. Church, M.L. McAdams and W.A. Pryor (1991) Free radical production from the ozonation of simple alkenes, fatty acid emulsions and phosphatidylcholine liposomes. In Oxidative Damage and Repair: Chemical, Biological and Medical Aspects (Ed. K.J.A. Davies), Pergamon Press, Oxford, pp. 517-522.
    • (1991) Oxidative Damage and Repair: Chemical, Biological and Medical Aspects , pp. 517-522
    • Church, D.F.1    McAdams, M.L.2    Pryor, W.A.3
  • 5
    • 0027475020 scopus 로고
    • A kinetic model for the competitive reactions of ozone with amino acid residues in proteins in reverse micelles
    • W.A. Pryor and R.M. Uppu (1993) A kinetic model for the competitive reactions of ozone with amino acid residues in proteins in reverse micelles. Journal of Biological Chemistry, 268, 3120-3126.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 3120-3126
    • Pryor, W.A.1    Uppu, R.M.2
  • 6
    • 0030070186 scopus 로고    scopus 로고
    • Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin
    • B.S. Berlett, R.L. Levine and E.R. Stadtman (1996) Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin. Journal of Biological Chemistry, 271, 4177-4182.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 4177-4182
    • Berlett, B.S.1    Levine, R.L.2    Stadtman, E.R.3
  • 8
    • 50549175610 scopus 로고
    • The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
    • J.T. Dodge, C. Mitchell and D.J. Hanahan (1963) The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Archives of Biochemistry and Biophysics, 100, 119-130.
    • (1963) Archives of Biochemistry and Biophysics , vol.100 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. Bradford (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 11
    • 0345646653 scopus 로고
    • The use of organic solvents in membrane research
    • (Ed. E. D. Korn), Plenum Press, New York and London
    • P. Zahler and V. Niggli (1977) The use of organic solvents in membrane research. In Methods in Membrane Biology (Ed. E. D. Korn), Plenum Press, New York and London, pp. 1-44.
    • (1977) Methods in Membrane Biology , pp. 1-44
    • Zahler, P.1    Niggli, V.2
  • 12
    • 0002144978 scopus 로고
    • Electron spin resonance analysis of model and biological membranes
    • (Eds. R.C. Abia, C.C. Curtain and L.M. Gordon), Alan R. Liss, Inc., New York
    • L.M. Gordon and C.C. Curtain (1988) Electron spin resonance analysis of model and biological membranes. In Methods for Studying Membrane Fluidity (Eds. R.C. Abia, C.C. Curtain and L.M. Gordon), Alan R. Liss, Inc., New York, pp. 25-88.
    • (1988) Methods for Studying Membrane Fluidity , pp. 25-88
    • Gordon, L.M.1    Curtain, C.C.2
  • 13
    • 0024424977 scopus 로고
    • Oxygen gradients in CHO cells: Measurement and characterization by electron spin resonance
    • J.F. Glockner, H.M. Swartz and MA. Pals (1989) Oxygen gradients in CHO cells: measurement and characterization by electron spin resonance. Journal of Cellular Physiology, 140, 505-511.
    • (1989) Journal of Cellular Physiology , vol.140 , pp. 505-511
    • Glockner, J.F.1    Swartz, H.M.2    Pals, M.A.3
  • 16
    • 0030934316 scopus 로고    scopus 로고
    • Stable nitroxide radicals protect lipid acyl chains from radiation damage
    • A.M. Samuni and Y. Barenholz (1997) Stable nitroxide radicals protect lipid acyl chains from radiation damage. Free Radicals in Biology and Medicine, 22, 1165-1174.
    • (1997) Free Radicals in Biology and Medicine , vol.22 , pp. 1165-1174
    • Samuni, A.M.1    Barenholz, Y.2
  • 22
    • 0029028275 scopus 로고
    • Self-peroxidation of metymyoglobin results in formation of an oxygen-reactive tryptophan-centered radical
    • M.R. Gunther, D.J. Kelman, J.T. Corbett and R.P. Mason (1995) Self-peroxidation of metymyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. Journal of Biological Chemistry, 270, 16075-16081.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 16075-16081
    • Gunther, M.R.1    Kelman, D.J.2    Corbett, J.T.3    Mason, R.P.4
  • 23
    • 0029900542 scopus 로고    scopus 로고
    • ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide
    • D.P. Barr, M.R. Gunther, L.J. Deterding, K.B. Tomer and R.P. Mason (1996) ESR Spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide. Journal of Biological Chemistry, 271, 15498-15503.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 15498-15503
    • Barr, D.P.1    Gunther, M.R.2    Deterding, L.J.3    Tomer, K.B.4    Mason, R.P.5
  • 25
    • 0029239723 scopus 로고
    • Rate constant for reaction of vitamin C with protein radicals in gamma irradiated aqueous albumin solution at 295 K
    • T. Miyazaki, T. Yoshimura, K. Mita, K. Suzuki and M. Watanabe (1995) Rate constant for reaction of vitamin C with protein radicals in gamma irradiated aqueous albumin solution at 295 K. Radiation Physics and Chemistry, 45, 199-202.
    • (1995) Radiation Physics and Chemistry , vol.45 , pp. 199-202
    • Miyazaki, T.1    Yoshimura, T.2    Mita, K.3    Suzuki, K.4    Watanabe, M.5
  • 26
    • 0032520869 scopus 로고    scopus 로고
    • Photodynamically generated bovine serum albumin radicals - Evidence for damage transfer and oxidation at cysteine and tryptophan residues
    • J.A. Silvester, G.S. Timmins and M.J. Davies (1998) Photodynamically generated bovine serum albumin radicals - evidence for damage transfer and oxidation at cysteine and tryptophan residues. Free Radicals in Biology and Medicine, 24, 754-766.
    • (1998) Free Radicals in Biology and Medicine , vol.24 , pp. 754-766
    • Silvester, J.A.1    Timmins, G.S.2    Davies, M.J.3
  • 27
    • 0030814598 scopus 로고    scopus 로고
    • Direct ESR detection of peroxynitrite-induced tyrosine-centered protein radicals in human blood plasma
    • D. Pietraforte and M. Minetti (1997) Direct ESR detection of peroxynitrite-induced tyrosine-centered protein radicals in human blood plasma. Biochemical Journal, 325, 675-684.
    • (1997) Biochemical Journal , vol.325 , pp. 675-684
    • Pietraforte, D.1    Minetti, M.2
  • 28
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical mediated protein oxidation
    • R.T. Dean, S.L. Fu, R. Stocker and M.J. Davies (1997) Biochemistry and pathology of radical mediated protein oxidation. Biochemical Journal, 324, 1-18.
    • (1997) Biochemical Journal , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.L.2    Stocker, R.3    Davies, M.J.4
  • 29
    • 0027194813 scopus 로고
    • Antioxidant activity of nitroxide radicals in lipid peroxidation of rat liver microsomes
    • Y. Miura, H. Utsumi and A. Hamada (1993) Antioxidant activity of nitroxide radicals in lipid peroxidation of rat liver microsomes. Archives of Biochemistry and Biophysics, 300, 148-156.
    • (1993) Archives of Biochemistry and Biophysics , vol.300 , pp. 148-156
    • Miura, Y.1    Utsumi, H.2    Hamada, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.