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Volumn 4, Issue 4, 2009, Pages

Changes in dry state hemoglobin over time do not increase the potential for oxidative DNA damage in dried blood

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBOSE; DNA; HEMOGLOBIN; HYDROXYL RADICAL; IRON; METHEMOGLOBIN; NUCLEIC ACID BASE; OXYHEMOGLOBIN;

EID: 65249085034     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005110     Document Type: Article
Times cited : (29)

References (43)
  • 2
    • 0023779695 scopus 로고
    • Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron
    • Puppo A, Halliwell B (1988) Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Biochem J 249: 185-190.
    • (1988) Biochem J , vol.249 , pp. 185-190
    • Puppo, A.1    Halliwell, B.2
  • 3
    • 0019502519 scopus 로고
    • Thiobarbituric acid-reactivity following iron-dependent free-radical damage to amino acids and carbohydrates
    • Gutteridge JMC (1981) Thiobarbituric acid-reactivity following iron-dependent free-radical damage to amino acids and carbohydrates. FEBS Letters 128: 343-346.
    • (1981) FEBS Letters , vol.128 , pp. 343-346
    • Gutteridge, J.M.C.1
  • 4
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity and oxidative stress
    • Valko M, Morris H, Cronin MT (2005) Metals, toxicity and oxidative stress. Curr Med Chem 12: 1161-1208.
    • (2005) Curr Med Chem , vol.12 , pp. 1161-1208
    • Valko, M.1    Morris, H.2    Cronin, M.T.3
  • 5
    • 0036968688 scopus 로고    scopus 로고
    • Iron transport: Emerging roles in health and disease
    • Goswami T, Rolfs A, Hediger MA (2002) Iron transport: emerging roles in health and disease. Biochem Cell Biol 80: 679-689.
    • (2002) Biochem Cell Biol , vol.80 , pp. 679-689
    • Goswami, T.1    Rolfs, A.2    Hediger, M.A.3
  • 6
    • 0034949363 scopus 로고    scopus 로고
    • Iron metabolism, free radicals, and oxidative injury
    • Emerit J, Beaumont C, Trivin F (2001) Iron metabolism, free radicals, and oxidative injury. Biomed Pharmacother 55: 333-339.
    • (2001) Biomed Pharmacother , vol.55 , pp. 333-339
    • Emerit, J.1    Beaumont, C.2    Trivin, F.3
  • 7
    • 33845944459 scopus 로고    scopus 로고
    • Hepatic oxidative DNA damage correlates with iron overload in chronic hepatitis C patients
    • Fujita N, Horiike S, Sugimoto R, Tanaka H, Iwasa M, et al. (2007) Hepatic oxidative DNA damage correlates with iron overload in chronic hepatitis C patients. Free Radical Biol Med 42: 353-362.
    • (2007) Free Radical Biol Med , vol.42 , pp. 353-362
    • Fujita, N.1    Horiike, S.2    Sugimoto, R.3    Tanaka, H.4    Iwasa, M.5
  • 8
    • 33645917671 scopus 로고    scopus 로고
    • Post-mortem DNA damage: A comparative study of STRs and SNPs typing efficiency in simulated forensic samples. Internaltion Congress Series
    • Onori N, Onofri V, Alessandrini F, Buscemi L, Pesaresi M, et al. (2006) Post-mortem DNA damage: A comparative study of STRs and SNPs typing efficiency in simulated forensic samples. Internaltion Congress Series: Progress in Forensic Genetics 11 1288: 510-512.
    • (2006) Progress in Forensic Genetics , vol.11 , Issue.1288 , pp. 510-512
    • Onori, N.1    Onofri, V.2    Alessandrini, F.3    Buscemi, L.4    Pesaresi, M.5
  • 9
    • 85023125114 scopus 로고    scopus 로고
    • Capillary electrophoresis reveals DNA damage in aged forensic samples. International Congress Series
    • Fattorini P, Tomasella F, Albertinie E, Grignani P, Previdere C (2004) Capillary electrophoresis reveals DNA damage in aged forensic samples. International Congress Series: Progress in Forensic Genetics 10 1261: 559-561.
    • (2004) Progress in Forensic Genetics , vol.10 , Issue.1261 , pp. 559-561
    • Fattorini, P.1    Tomasella, F.2    Albertinie, E.3    Grignani, P.4    Previdere, C.5
  • 10
    • 0017822690 scopus 로고
    • Mechanism of oxyhaemoglobin breakdown on reaction with acetylphenylhydrazine
    • French JK, Winterbourn CC, Carrell RW (1978) Mechanism of oxyhaemoglobin breakdown on reaction with acetylphenylhydrazine. Biochem J 173: 19-29.
    • (1978) Biochem J , vol.173 , pp. 19-29
    • French, J.K.1    Winterbourn, C.C.2    Carrell, R.W.3
  • 11
    • 0025145949 scopus 로고
    • Oxidation Reactions of Hemoglobin
    • Winterbourn CC (1990) Oxidation Reactions of Hemoglobin. Methods Enzymol 186: 265-272.
    • (1990) Methods Enzymol , vol.186 , pp. 265-272
    • Winterbourn, C.C.1
  • 12
    • 0018145231 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates
    • Halliwell B (1978) Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates. FEBS Letters 92: 321-326.
    • (1978) FEBS Letters , vol.92 , pp. 321-326
    • Halliwell, B.1
  • 13
    • 0021764939 scopus 로고
    • Reactivity of hydroxyl and hydroxyl-like radicals discriminated by release of thiobarbituric acid-reactive material from deoxy sugars, nucleosides and benzoate
    • Gutteridge JMC (1984) Reactivity of hydroxyl and hydroxyl-like radicals discriminated by release of thiobarbituric acid-reactive material from deoxy sugars, nucleosides and benzoate. Biochem J 224: 761-767.
    • (1984) Biochem J , vol.224 , pp. 761-767
    • Gutteridge, J.M.C.1
  • 14
    • 0025370786 scopus 로고
    • Superoxide dismutase and Fenton chemistry
    • Gutteridge JMC, Maidt L, Poyer L (1990) Superoxide dismutase and Fenton chemistry. Biochem J 269: 169-174.
    • (1990) Biochem J , vol.269 , pp. 169-174
    • Gutteridge, J.M.C.1    Maidt, L.2    Poyer, L.3
  • 15
    • 0019881197 scopus 로고
    • Formation of thiobarbituric-acid-reactive substance from deoxyribose in the present of iron salts
    • Gutteridge JMC, Halliwell B (1981) Formation of thiobarbituric-acid-reactive substance from deoxyribose in the present of iron salts. FEBS Letters 128: 347-352.
    • (1981) FEBS Letters , vol.128 , pp. 347-352
    • Gutteridge, J.M.C.1    Halliwell, B.2
  • 16
    • 0022454517 scopus 로고
    • Copper+zinc and manganese superoxide dismutases inhibit deoxyribose degradation by the superoxide-driven Fenton reaction at two different stages
    • Gutteridge JMC, Bannister JV (1986) Copper+zinc and manganese superoxide dismutases inhibit deoxyribose degradation by the superoxide-driven Fenton reaction at two different stages. Biochem J 234: 225-228.
    • (1986) Biochem J , vol.234 , pp. 225-228
    • Gutteridge, J.M.C.1    Bannister, J.V.2
  • 17
    • 0021793987 scopus 로고
    • Superoxide dismutase inhibits the superoxide-driven Fenton reaction at two different levels
    • Gutteridge JMC (1985) Superoxide dismutase inhibits the superoxide-driven Fenton reaction at two different levels. FEBS Letters 185: 19-23.
    • (1985) FEBS Letters , vol.185 , pp. 19-23
    • Gutteridge, J.M.C.1
  • 18
    • 0023779695 scopus 로고
    • Formation of Hydroxyl Radicals from Hydrogen-Peroxide in the Presence of Iron - Is Hemoglobin A Biological Fenton Reagent
    • Puppo A, Halliwell B (1988) Formation of Hydroxyl Radicals from Hydrogen-Peroxide in the Presence of Iron - Is Hemoglobin A Biological Fenton Reagent. Biochem J 249: 185-190.
    • (1988) Biochem J , vol.249 , pp. 185-190
    • Puppo, A.1    Halliwell, B.2
  • 19
    • 0023219256 scopus 로고
    • The deoxyribose method: A simple 'test-tube' assay for determination of rate constants for reactions of hydroxyl radicals
    • Halliwell B, Gutteridge JMC, Aruoma OI (1987) The deoxyribose method: A simple 'test-tube' assay for determination of rate constants for reactions of hydroxyl radicals. Anal Biochem 165: 216-219.
    • (1987) Anal Biochem , vol.165 , pp. 216-219
    • Halliwell, B.1    Gutteridge, J.M.C.2    Aruoma, O.I.3
  • 20
    • 0022469346 scopus 로고
    • Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides
    • Gutteridge JMC (1986) Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Letters 201: 291-295.
    • (1986) FEBS Letters , vol.201 , pp. 291-295
    • Gutteridge, J.M.C.1
  • 21
    • 0015239545 scopus 로고
    • Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives
    • Rachmilewitz EA, Peisach J, Blumberg WE (1971) Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives. J Biol Chem 246: 3356-3366.
    • (1971) J Biol Chem , vol.246 , pp. 3356-3366
    • Rachmilewitz, E.A.1    Peisach, J.2    Blumberg, W.E.3
  • 22
    • 0015040637 scopus 로고
    • Spectrophotometric Determination of Serum Iron at Submicrogram Level with A New Reagent (Ferrozine)
    • Carter P (1971) Spectrophotometric Determination of Serum Iron at Submicrogram Level with A New Reagent (Ferrozine). Anal Biochem 40: 450.
    • (1971) Anal Biochem , vol.40 , pp. 450
    • Carter, P.1
  • 23
    • 33847670407 scopus 로고
    • Ferrozine - A new spectrophotometric reagent for iron
    • Stookey LL (1970) Ferrozine - A new spectrophotometric reagent for iron. Anal Chem 72: 779.
    • (1970) Anal Chem , vol.72 , pp. 779
    • Stookey, L.L.1
  • 24
    • 14844282103 scopus 로고    scopus 로고
    • Spectrophotometric determination of ascorbic acid using copper(II)-neocuproine reagent in beverages and pharmaceuticals
    • Guclu K, Sozgen K, Tutem E, Ozyurek M, Apak R (2005) Spectrophotometric determination of ascorbic acid using copper(II)-neocuproine reagent in beverages and pharmaceuticals. Talanta 65: 1226-1232.
    • (2005) Talanta , vol.65 , pp. 1226-1232
    • Guclu, K.1    Sozgen, K.2    Tutem, E.3    Ozyurek, M.4    Apak, R.5
  • 25
    • 31344436398 scopus 로고    scopus 로고
    • Spectrophotometric total protein assay with copper(II)-neocuproine reagent in alkaline medium
    • Sozgen K, Cekic SD, Tutem E, Apak R (2005) Spectrophotometric total protein assay with copper(II)-neocuproine reagent in alkaline medium. Talanta 68: 1601-1609.
    • (2005) Talanta , vol.68 , pp. 1601-1609
    • Sozgen, K.1    Cekic, S.D.2    Tutem, E.3    Apak, R.4
  • 26
    • 0022939235 scopus 로고
    • An aromatic hydroxylation assay for hydroxyl radicals utilizing high-performance liquid chromatography (HPLC). Use to investigate the effect of EDTA on the Fenton reaction
    • Grootveld M, Halliwell B (1986) An aromatic hydroxylation assay for hydroxyl radicals utilizing high-performance liquid chromatography (HPLC). Use to investigate the effect of EDTA on the Fenton reaction. Free Rad Res Comm 1: 243-250.
    • (1986) Free Rad Res Comm , vol.1 , pp. 243-250
    • Grootveld, M.1    Halliwell, B.2
  • 27
    • 0022406392 scopus 로고
    • Cobalt(II) ion as a promoter of hydroxyl radical and possible 'crypto-hydroxyl' radical formation under physiological conditions. Differential effects of hydroxyl raical scavengers
    • Moorhouse CP, Halliwell B, Grootveld M, Gutteridge JMC (1985) Cobalt(II) ion as a promoter of hydroxyl radical and possible 'crypto-hydroxyl' radical formation under physiological conditions. Differential effects of hydroxyl raical scavengers. Biochim Biophys Acta 843: 261-268.
    • (1985) Biochim Biophys Acta , vol.843 , pp. 261-268
    • Moorhouse, C.P.1    Halliwell, B.2    Grootveld, M.3    Gutteridge, J.M.C.4
  • 28
    • 0024061286 scopus 로고
    • The deoxyribose assay: An assay both for 'free' hydroxyl radical and for site-specific hydroxyl radical production
    • Gutteridge JMC, Halliwell B (1988) The deoxyribose assay: an assay both for 'free' hydroxyl radical and for site-specific hydroxyl radical production. Biochem J Lett 253: 932-933.
    • (1988) Biochem J Lett , vol.253 , pp. 932-933
    • Gutteridge, J.M.C.1    Halliwell, B.2
  • 29
    • 0023779695 scopus 로고
    • Formation of Hydroxyl Radicals from Hydrogen-Peroxide in the Presence of Iron - Is Hemoglobin A Biological Fenton Reagent
    • Puppo A, Halliwell B (1988) Formation of Hydroxyl Radicals from Hydrogen-Peroxide in the Presence of Iron - Is Hemoglobin A Biological Fenton Reagent. Biochem J 249: 185-190.
    • (1988) Biochem J , vol.249 , pp. 185-190
    • Puppo, A.1    Halliwell, B.2
  • 30
    • 0022553634 scopus 로고
    • Formation of hydroxyl radicals in the presence of ferritine and haemosiderin
    • O'Connell M, Halliwell B, Moorhouse CP, Aruoma OI (1986) Formation of hydroxyl radicals in the presence of ferritine and haemosiderin. Biochem J 234: 727-731.
    • (1986) Biochem J , vol.234 , pp. 727-731
    • O'Connell, M.1    Halliwell, B.2    Moorhouse, C.P.3    Aruoma, O.I.4
  • 31
    • 0019847498 scopus 로고
    • Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts
    • Gutteridge JMC, Rowley DA, Halliwell B (1981) Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Biochem J 199: 263-265.
    • (1981) Biochem J , vol.199 , pp. 263-265
    • Gutteridge, J.M.C.1    Rowley, D.A.2    Halliwell, B.3
  • 32
    • 0022931569 scopus 로고
    • Aspects to consider when detecting and measuring lipid peroxidation
    • Gutteridge JMC (1986) Aspects to consider when detecting and measuring lipid peroxidation. Free Rad Res Comm 1: 173-184.
    • (1986) Free Rad Res Comm , vol.1 , pp. 173-184
    • Gutteridge, J.M.C.1
  • 33
    • 0021684774 scopus 로고
    • The thiobarbituric acid test for lipid peroxidation: Structure of the adduct with malondialdehyde
    • Nair V, Turner GA (1984) The thiobarbituric acid test for lipid peroxidation: structure of the adduct with malondialdehyde. Lipids 19: 804-805.
    • (1984) Lipids , vol.19 , pp. 804-805
    • Nair, V.1    Turner, G.A.2
  • 34
    • 0018168171 scopus 로고
    • The characterisation of thiobarbituric acid reactivity in human plasma and urine
    • Gutteridge JMC, Tickner TR (1978) The characterisation of thiobarbituric acid reactivity in human plasma and urine. Anal Biochem 91: 250-257.
    • (1978) Anal Biochem , vol.91 , pp. 250-257
    • Gutteridge, J.M.C.1    Tickner, T.R.2
  • 35
    • 0023338482 scopus 로고
    • Ferrous-salt-promoted damage to deoxyribose and benzoate
    • Gutteridge JMC (1987) Ferrous-salt-promoted damage to deoxyribose and benzoate. Biochem J 243: 709-714.
    • (1987) Biochem J , vol.243 , pp. 709-714
    • Gutteridge, J.M.C.1
  • 36
    • 0020463385 scopus 로고
    • Iron-dependent free radical damage to DNA and deoxyribose separation of TBA-reactive intermediates
    • Gutteridge JMC, Toeg D (1982) Iron-dependent free radical damage to DNA and deoxyribose separation of TBA-reactive intermediates. Int J Biochem 14: 891-893.
    • (1982) Int J Biochem , vol.14 , pp. 891-893
    • Gutteridge, J.M.C.1    Toeg, D.2
  • 37
    • 0021735773 scopus 로고
    • Ferrous ion-EDTA-stimulated phospholipid peroxidation
    • Gutteridge JMC (1984) Ferrous ion-EDTA-stimulated phospholipid peroxidation. Biochem J 224: 697-701.
    • (1984) Biochem J , vol.224 , pp. 697-701
    • Gutteridge, J.M.C.1
  • 38
    • 0021142628 scopus 로고
    • Lipid peroxidation initiated by superoxide-dependent hydroxyl radicals using complexed iron and hydrogen peroxide
    • Gutteridge JMC (1984) Lipid peroxidation initiated by superoxide-dependent hydroxyl radicals using complexed iron and hydrogen peroxide. FEBS Letters 172: 245-249.
    • (1984) FEBS Letters , vol.172 , pp. 245-249
    • Gutteridge, J.M.C.1
  • 41
    • 0017113866 scopus 로고
    • Reactions involving superoxide and normal and unstable haemoglobins
    • Winterbourn CC, McGrath BM, Carrell RW (1976) Reactions involving superoxide and normal and unstable haemoglobins. Biochem J 155: 493-502.
    • (1976) Biochem J , vol.155 , pp. 493-502
    • Winterbourn, C.C.1    McGrath, B.M.2    Carrell, R.W.3
  • 42
    • 0019765114 scopus 로고
    • Preparation of blood hemoglobins of vertebrates
    • Riggs A (1981) Preparation of blood hemoglobins of vertebrates. Methods Enzymol 76: 5-29.
    • (1981) Methods Enzymol , vol.76 , pp. 5-29
    • Riggs, A.1
  • 43
    • 0020490335 scopus 로고
    • Redox transformation in ferrimyoglobin induced by radiation-generated free radicals in aqueous solution
    • Whitburn KD, Shieh JJ, Sellers RM, Hoffman MZ, Taub IA (1982) Redox transformation in ferrimyoglobin induced by radiation-generated free radicals in aqueous solution. J Biol Chem 257: 1860-1869.
    • (1982) J Biol Chem , vol.257 , pp. 1860-1869
    • Whitburn, K.D.1    Shieh, J.J.2    Sellers, R.M.3    Hoffman, M.Z.4    Taub, I.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.