메뉴 건너뛰기




Volumn 267, Issue 1-2, 2004, Pages 195-201

Influence of plasma total antioxidant ability on lipid and protein oxidation products in plasma and erythrocyte ghost obtained from developing and adult rats pretreated with two vitamin K formulations

Author keywords

Erythrocyte ghost; FRAP; Lipid peroxidation; Menadione; Plasma; Protein oxidation; SDS PAGE; Vitamin K1

Indexed keywords

CARBONYL DERIVATIVE; FERRIC ION; MEMBRANE PROTEIN; MENADIONE; PHYTOMENADIONE; THIOBARBITURIC ACID REACTIVE SUBSTANCE;

EID: 9444223296     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MCBI.0000049383.94541.31     Document Type: Article
Times cited : (3)

References (31)
  • 2
    • 0021671419 scopus 로고
    • Alterations in intracellular thiol homeostasis during the metabolism of menadione by isolated rat hepatocytes
    • Di Monte D, Ross D, Bellomo G, Eklow L, Orrinius S: Alterations in intracellular thiol homeostasis during the metabolism of menadione by isolated rat hepatocytes. Arch Biochem Biophys 235: 334-342, 1984
    • (1984) Arch. Biochem. Biophys. , vol.235 , pp. 334-342
    • Di Monte, D.1    Ross, D.2    Bellomo, G.3    Eklow, L.4    Orrinius, S.5
  • 4
    • 0023790206 scopus 로고
    • Alterations of surface morphology caused by the metabolism of menadione in mammalian cells are associated with the oxidation of critical sulfhydryl groups in cytoskeletal proteins
    • Mirabelli F, Salis A, Perotti M, Taddei F, Bellomo G, Orrinius S: Alterations of surface morphology caused by the metabolism of menadione in mammalian cells are associated with the oxidation of critical sulfhydryl groups in cytoskeletal proteins. Biochem Pharmacol 37: 3423-3427, 1988
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 3423-3427
    • Mirabelli, F.1    Salis, A.2    Perotti, M.3    Taddei, F.4    Bellomo, G.5    Orrinius, S.6
  • 6
    • 0022907585 scopus 로고
    • In vivo synergy of vitamin K3 and methotrexate in tumor bearing animals
    • Gold J: In vivo synergy of vitamin K3 and methotrexate in tumor bearing animals. Cancer treat Rep 70: 1433-1435, 1986
    • (1986) Cancer Treat. Rep. , vol.70 , pp. 1433-1435
    • Gold, J.1
  • 8
    • 0024592332 scopus 로고
    • Free radical formation by antitumor quinones
    • Powis G: Free radical formation by antitumor quinones. Free Radic Biol Med 6: 63-101, 1989
    • (1989) Free Radic. Biol. Med. , vol.6 , pp. 63-101
    • Powis, G.1
  • 11
    • 0001638069 scopus 로고    scopus 로고
    • Developmental homeostasis relevance to newborns and infants
    • DG Nathan, SH Orkin (eds). W. B. Saunders, Philadelphia
    • Andrew A: Developmental homeostasis relevance to newborns and infants. In: DG Nathan, SH Orkin (eds). Nathan and Oski's Hematology of Infancy and Childhood, W. B. Saunders, Philadelphia, 1998, pp 114-157
    • (1998) Nathan and Oski's Hematology of Infancy and Childhood , pp. 114-157
    • Andrew, A.1
  • 12
    • 0001613399 scopus 로고
    • Neonatology, Pathophysiology and Management of the newborn
    • GB Avery, MA Fletcher, MG Mac Donald (eds). J.B. Lippincot and Co. Philadelphia
    • Blanchett V, Doyle J, Schmidt B, Zippursky A: Neonatology, Pathophysiology and Management of the newborn. In: GB Avery, MA Fletcher, MG Mac Donald (eds). Hematology. J.B. Lippincot and Co. Philadelphia, 1994, pp. 952-999
    • (1994) Hematology , pp. 952-999
    • Blanchett, V.1    Doyle, J.2    Schmidt, B.3    Zippursky, A.4
  • 13
    • 0022458970 scopus 로고
    • Presence of phosphatidylserin in the outer membrane bilayer of new-born human erythrocyte
    • Jain SK: Presence of phosphatidylserin in the outer membrane bilayer of new-born human erythrocyte. Biochem Biophys Res Commun 136: 914-920, 1986
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , pp. 914-920
    • Jain, S.K.1
  • 14
    • 0028889025 scopus 로고
    • Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism
    • Cadenas E: Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism. Biochem Pharmacol 49P 127-140, 1995
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 127-140
    • Cadenas, E.1
  • 15
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • O'Brien PJ: Molecular mechanisms of quinone cytotoxicity. Chem Biol Interac 80: 1-14, 1991
    • (1991) Chem. Biol. Interac. , vol.80 , pp. 1-14
    • O'Brien, P.J.1
  • 16
    • 0031029955 scopus 로고    scopus 로고
    • Autooxidation of naphthohydroquinones: Effects of metals, chelating agents and superoxide dismutase
    • Munday R: Autooxidation of naphthohydroquinones: Effects of metals, chelating agents and superoxide dismutase. Free Radic Biol Med 22: 689-695, 1997
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 689-695
    • Munday, R.1
  • 17
    • 0037154406 scopus 로고    scopus 로고
    • The pro-oxidant role of protein SH groups of hemoglobin in rat erythrocytes exposed to menadione
    • Lusini L, Rossi R, Giustarini D, Di Simplicio P: The pro-oxidant role of protein SH groups of hemoglobin in rat erythrocytes exposed to menadione. Chemico Biol Interact 139: 97-114, 2002
    • (2002) Chemico Biol. Interact. , vol.139 , pp. 97-114
    • Lusini, L.1    Rossi, R.2    Giustarini, D.3    Di Simplicio, P.4
  • 18
    • 0024451403 scopus 로고
    • The neonatal erythrocyte and its oxidative susceptibility
    • Jain SK: The neonatal erythrocyte and its oxidative susceptibility. Semin Hematol 26: 286-300, 1989
    • (1989) Semin. Hematol. , vol.26 , pp. 286-300
    • Jain, S.K.1
  • 19
    • 0009712442 scopus 로고    scopus 로고
    • Preparation of human erythrocyte ghosts
    • JE Celis (ed). 2nd edn Academic Press
    • Shotton DM: Preparation of human erythrocyte ghosts. In: JE Celis (ed). Cell Biology, A Laboratory Handbook, 2nd edn, Vol. 2, Academic Press, 1998, pp 26-33
    • (1998) Cell Biology, A Laboratory Handbook , vol.2 , pp. 26-33
    • Shotton, D.M.1
  • 20
    • 0000470054 scopus 로고
    • Spectrophotometric studies, spectrophotometric constants for common hemoglobin derivatives in human, dog and rabbit blood
    • Drabkin DL, Austin JM: Spectrophotometric studies, spectrophotometric constants for common hemoglobin derivatives in human, dog and rabbit blood. J Biol Chem 98: 719-733, 1932
    • (1932) J. Biol. Chem. , vol.98 , pp. 719-733
    • Drabkin, D.L.1    Austin, J.M.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bactriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bactriophage T4. Nature 227: 680-685, 1970
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0001211208 scopus 로고    scopus 로고
    • Peroxides and other products
    • Punchard and Kelly (eds). IRL Press, Oxford University Press
    • Brown RK, Kelly FJ: Peroxides and other products. In: Punchard and Kelly (eds). Free radicals: A practical approach. IRL Press, Oxford University Press, 1996
    • (1996) Free Radicals: A Practical Approach
    • Brown, R.K.1    Kelly, F.J.2
  • 23
    • 0031797254 scopus 로고    scopus 로고
    • Measurements of protein carbonyls in human brain tissue
    • Academic Press
    • Evans P: Measurements of protein carbonyls in human brain tissue. In: Methods in Enzymology, Vol. 300, Academic Press, 1999
    • (1999) Methods in Enzymology , vol.300
    • Evans, P.1
  • 24
    • 0030586361 scopus 로고    scopus 로고
    • The ferric reducing ability of plasma (FRAP) as a measure of antioxidant power: The FRAP assay
    • Benzie IFF, Strain JJ: The ferric reducing ability of plasma (FRAP) as a measure of antioxidant power: The FRAP assay. Analytical Biochem 239: 70-76, 1996
    • (1996) Analytical Biochem. , vol.239 , pp. 70-76
    • Benzie, I.F.F.1    Strain, J.J.2
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochem 72: 248-254, 1976
    • (1976) Analytical Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 9444275051 scopus 로고
    • Red cell metabolism in the new-born infant. IV. Irreversible oxidant nutrients
    • Lubin B, Oski FA: Red cell metabolism in the new-born infant. IV. Irreversible oxidant nutrients. FASEB J 1: 441-445, 1972
    • (1972) FASEB J. , vol.1 , pp. 441-445
    • Lubin, B.1    Oski, F.A.2
  • 27
    • 84957294043 scopus 로고
    • Superoxide dismutase, catalase and glutathione peroxidase activities in maternal and cord blood erythrocytes
    • Agostini A, Gerli GC, Beretta L: Superoxide dismutase, catalase and glutathione peroxidase activities in maternal and cord blood erythrocytes. J Clin Chem Clin Biochem 18: 771-773, 1980
    • (1980) J. Clin. Chem. Clin. Biochem. , vol.18 , pp. 771-773
    • Agostini, A.1    Gerli, G.C.2    Beretta, L.3
  • 28
    • 0035054722 scopus 로고    scopus 로고
    • High sensitivity to autooxidation in neonatal calf erythrocytes: Possible mechanism of accelerated cell ageing
    • Imre S, Csornai M, Balazs M: High sensitivity to autooxidation in neonatal calf erythrocytes: Possible mechanism of accelerated cell ageing. Mechanisms Ageing Dev 122: 69-76, 2001
    • (2001) Mechanisms Ageing Dev. , vol.122 , pp. 69-76
    • Imre, S.1    Csornai, M.2    Balazs, M.3
  • 29
    • 0034706929 scopus 로고    scopus 로고
    • The roles of glutathione and antioxidant enzymes in menadione-induced oxidative stress
    • Chiou TJ, Tzeng WF: The roles of glutathione and antioxidant enzymes in menadione-induced oxidative stress. Toxicology 154: 75-84, 2000
    • (2000) Toxicology , vol.154 , pp. 75-84
    • Chiou, T.J.1    Tzeng, W.F.2
  • 30
    • 0024468158 scopus 로고
    • Lipid peroxidation in human red cells
    • Chiu D, Kuypers F, Lubin B: Lipid peroxidation in human red cells. Semin Hematol 26: 257-276, 1989
    • (1989) Semin. Hematol. , vol.26 , pp. 257-276
    • Chiu, D.1    Kuypers, F.2    Lubin, B.3
  • 31
    • 0031745637 scopus 로고    scopus 로고
    • Comparison of different analytical methods for assessing total antioxidant capacity of human serum
    • Cao G, Prior RL: Comparison of different analytical methods for assessing total antioxidant capacity of human serum. Clin Chem 44: 1309-1315, 1998
    • (1998) Clin. Chem. , vol.44 , pp. 1309-1315
    • Cao, G.1    Prior, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.