메뉴 건너뛰기




Volumn 50, Issue 1, 2007, Pages 84-90

SDS-PAGE study on photooxidation damage of lysozyme induced by riboflavin

Author keywords

Antioxidant; Lysozyme; Photooxidation; Riboflavin; SDS PAGE

Indexed keywords

AMIDES; CONCENTRATION (PROCESS); ELECTROPHORESIS; PHOTOOXIDATION; SODIUM COMPOUNDS; VITAMINS;

EID: 34547225135     PISSN: 10069291     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11426-007-0014-z     Document Type: Article
Times cited : (7)

References (25)
  • 2
    • 37049105153 scopus 로고
    • The photophysical and photochemical properties of ribofalvins (isoalloxazines)
    • Heelis R F. The photophysical and photochemical properties of ribofalvins (isoalloxazines). Chem Soc Rev, 1982, 11:15-39
    • (1982) Chem Soc Rev , vol.11 , pp. 15-39
    • Heelis, R.F.1
  • 3
    • 0026251573 scopus 로고
    • Definition of type I and type II photosensitized oxidation
    • Foote C S. Definition of type I and type II photosensitized oxidation. Photochem Photobiol, 1991, 54(5): 659
    • (1991) Photochem Photobiol , vol.54 , Issue.5 , pp. 659
    • Foote, C.S.1
  • 4
    • 0028230709 scopus 로고
    • Riboflavin-sensitized photoprocesses of tryptophan
    • Silva E, Ugarte R, Andrade A, et al. Riboflavin-sensitized photoprocesses of tryptophan. J Photoch Photobio B, 1994, 23:43-48
    • (1994) J Photoch Photobio B , vol.23 , pp. 43-48
    • Silva, E.1    Ugarte, R.2    Andrade, A.3
  • 5
    • 0023914317 scopus 로고
    • Tryptophan-riboflavin photoinduced adduct and hepatic dysfunction in rats
    • Donoso M N, Valenzuela A, Silva E. Tryptophan-riboflavin photoinduced adduct and hepatic dysfunction in rats. Nutr Rep Int, 1988,37:599-606
    • (1988) Nutr Rep Int , vol.37 , pp. 599-606
    • Donoso, M.N.1    Valenzuela, A.2    Silva, E.3
  • 6
    • 0027490583 scopus 로고
    • 8-hydroxydeoxyguanosine formation at the 5' site of 5'-GG-3' sequences in double-stranded DNA by UV radiation with riboflavin
    • Ito K, Inoue S, Yamamoto K, et al. 8-hydroxydeoxyguanosine formation at the 5' site of 5'-GG-3' sequences in double-stranded DNA by UV radiation with riboflavin. J Biol Chem, 1993, 268(18): 13221-13227
    • (1993) J Biol Chem , vol.268 , Issue.18 , pp. 13221-13227
    • Ito, K.1    Inoue, S.2    Yamamoto, K.3
  • 7
    • 34547197455 scopus 로고    scopus 로고
    • The study on photo-induced DNA damage enhanced by riboflavin
    • Zhang L W, Lin W Z, Pan J X, et al. The study on photo-induced DNA damage enhanced by riboflavin. Sci China Ser C-Life Sci (in Chinese), 2001, 31(2): 178-184
    • (2001) Sci China Ser C-Life Sci (in Chinese) , vol.31 , Issue.2 , pp. 178-184
    • Zhang, L.W.1    Lin, W.Z.2    Pan, J.X.3
  • 8
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals (I): General aspects
    • Davies K J A. Protein damage and degradation by oxygen radicals (I): General aspects. J Biol Chem, 1987, 262(20): 9895-9901
    • (1987) J Biol Chem , vol.262 , Issue.20 , pp. 9895-9901
    • Davies, K.J.A.1
  • 9
    • 0034105326 scopus 로고    scopus 로고
    • Reactivity of monoclonal antibodies against a tryptophanriboflavin adduct toward irradialed and non-irradiated bovine-eye-lens protein fractions: An indicator of in vivo visible-light-mediated phototransformations
    • Mancini M, Edwards A M, Becker M I, et al. Reactivity of monoclonal antibodies against a tryptophanriboflavin adduct toward irradialed and non-irradiated bovine-eye-lens protein fractions: An indicator of in vivo visible-light-mediated phototransformations. J Photoch Photobio B, 2000, 55: 9-15
    • (2000) J Photoch Photobio B , vol.55 , pp. 9-15
    • Mancini, M.1    Edwards, A.M.2    Becker, M.I.3
  • 10
    • 0027965511 scopus 로고
    • Visible light effects on tumoral cells in a culture medium enriched with tryptophan and riboflavin
    • Edwards A M, Silva E, Jofré B, et al. Visible light effects on tumoral cells in a culture medium enriched with tryptophan and riboflavin. J Photoch Photobio B, 1994, 240(3): 179-186
    • (1994) J Photoch Photobio B , vol.240 , Issue.3 , pp. 179-186
    • Edwards, A.M.1    Silva, E.2    Jofré, B.3
  • 11
    • 34547180966 scopus 로고    scopus 로고
    • Goodrich R P. Cambridge Healthtech Institute's Sixth Annual Blood Product Safety Conference. 2000
    • Goodrich R P. Cambridge Healthtech Institute's Sixth Annual Blood Product Safety Conference. 2000
  • 12
    • 33744873175 scopus 로고    scopus 로고
    • Fast repair of purine deoxynucleotide radical cations by rutin and quercetin
    • Zhao C Y, Shi Y M, Wang W F, et al. Fast repair of purine deoxynucleotide radical cations by rutin and quercetin. Sci China Ser C-Life Sci, 2001, 44(6): 610-617
    • (2001) Sci China Ser C-Life Sci , vol.44 , Issue.6 , pp. 610-617
    • Zhao, C.Y.1    Shi, Y.M.2    Wang, W.F.3
  • 13
    • 33748695134 scopus 로고    scopus 로고
    • Transient species and its properties of melatonin
    • Zhu H P, Zhang Z X, Zhao H W, et al. Transient species and its properties of melatonin. Sci China Ser B-Chem, 2006, 49(4): 308-314
    • (2006) Sci China Ser B-Chem , vol.49 , Issue.4 , pp. 308-314
    • Zhu, H.P.1    Zhang, Z.X.2    Zhao, H.W.3
  • 14
    • 0033020990 scopus 로고    scopus 로고
    • Singlet oxygen quenching and the redox properties of hydroxycinnamic acids
    • Foley S, Navaratnam S, Mcgarvey D J, et al. Singlet oxygen quenching and the redox properties of hydroxycinnamic acids. Free Radical Bio Med, 1999, 26:1202-1208
    • (1999) Free Radical Bio Med , vol.26 , pp. 1202-1208
    • Foley, S.1    Navaratnam, S.2    Mcgarvey, D.J.3
  • 15
    • 23744469411 scopus 로고    scopus 로고
    • Kinetic study of the quenching reaction of singlet oxygen by tea catechins in ethanol solution
    • Mukai K, Nagai S, Ohara K. Kinetic study of the quenching reaction of singlet oxygen by tea catechins in ethanol solution. Free Radical Bio Med, 2005, 39: 752-761
    • (2005) Free Radical Bio Med , vol.39 , pp. 752-761
    • Mukai, K.1    Nagai, S.2    Ohara, K.3
  • 16
    • 0020572998 scopus 로고
    • L-ascorbic acid quenching of singlet delta molecular oxygen in aqueous media: Generalized antioxidant property of vitamin C
    • Chou P-T, Khan A U. L-ascorbic acid quenching of singlet delta molecular oxygen in aqueous media: Generalized antioxidant property of vitamin C. Biochem Bioph Res Co, 1983, 115: 932-937
    • (1983) Biochem Bioph Res Co , vol.115 , pp. 932-937
    • Chou, P.-T.1    Khan, A.U.2
  • 17
    • 0035906337 scopus 로고    scopus 로고
    • Vitamin C and gonomic stability
    • Halliwell B. Vitamin C and gonomic stability. Mutat Res, 2001, 475: 29-35
    • (2001) Mutat Res , vol.475 , pp. 29-35
    • Halliwell, B.1
  • 18
    • 34547164531 scopus 로고    scopus 로고
    • Lu C Y. Studies on the photo- and radio- sensitization mechanism of DNA and related biomilecules by riboflavin and flavin adenine dinudeotide (FAD) (in Chinese). Dissertation for the Doctoral Degree. Beijing: Chinese Academy of Science, 2000
    • Lu C Y. Studies on the photo- and radio- sensitization mechanism of DNA and related biomilecules by riboflavin and flavin adenine dinudeotide (FAD) (in Chinese). Dissertation for the Doctoral Degree. Beijing: Chinese Academy of Science, 2000
  • 19
    • 0024384199 scopus 로고
    • Pulse radiolytic measurement of redox potentials: The tyrosine and tryptophan radicals
    • DeFlippis M R, Murthy C P, Faraggi M, et al. Pulse radiolytic measurement of redox potentials: The tyrosine and tryptophan radicals. Biochem, 1989, 28:4847-4853
    • (1989) Biochem , vol.28 , pp. 4847-4853
    • DeFlippis, M.R.1    Murthy, C.P.2    Faraggi, M.3
  • 20
    • 0031027125 scopus 로고    scopus 로고
    • How easily oxidizable is DNA one-electron reduction potentials of adenosine and guanosine radicals in aqueous solution
    • Steenken S, Jovanovic S V. How easily oxidizable is DNA one-electron reduction potentials of adenosine and guanosine radicals in aqueous solution. J Am Chem Soc, 1997, 119: 617-618
    • (1997) J Am Chem Soc , vol.119 , pp. 617-618
    • Steenken, S.1    Jovanovic, S.V.2
  • 21
    • 0013852463 scopus 로고    scopus 로고
    • Blake C C F, Koenig D F, Mair G A, et al. Structure of hen egg-white lysozyme. A three-dimen-sional Fourier synthesis at 2 A resolution.Nature, 1965, 206: 757-763
    • Blake C C F, Koenig D F, Mair G A, et al. Structure of hen egg-white lysozyme. A three-dimen-sional Fourier synthesis at 2 A resolution.Nature, 1965, 206: 757-763
  • 22
    • 0022527517 scopus 로고
    • Exposure of tryptophanyl residues in α-lactalbumin and lysozyme. Quantitative determination by fluorescence quenching studies
    • Edwards A M, Silva E. Exposure of tryptophanyl residues in α-lactalbumin and lysozyme. Quantitative determination by fluorescence quenching studies. Radiat Environ Bioph, 1986, 25:113-122
    • (1986) Radiat Environ Bioph , vol.25 , pp. 113-122
    • Edwards, A.M.1    Silva, E.2
  • 23
    • 0026195330 scopus 로고
    • A study of the photodynamic efficcncies of some eye lens constituents
    • Krishna C M, Uppuluri S, Riesz P, et al. A study of the photodynamic efficcncies of some eye lens constituents. Photochem Photobiol, 1991, 54:51-58
    • (1991) Photochem Photobiol , vol.54 , pp. 51-58
    • Krishna, C.M.1    Uppuluri, S.2    Riesz, P.3
  • 25
    • 0037451636 scopus 로고    scopus 로고
    • Protection against oxidative protein damage induced by metal-catalyzed reaction or alkylperoxyl radicals: Comparative effects of melatonin and other antioxidants
    • Mayo J C, Tan D X, Sainz R M, et al. Protection against oxidative protein damage induced by metal-catalyzed reaction or alkylperoxyl radicals: Comparative effects of melatonin and other antioxidants. Biochim Biophys Acta, 2003, 1620: 139-150
    • (2003) Biochim Biophys Acta , vol.1620 , pp. 139-150
    • Mayo, J.C.1    Tan, D.X.2    Sainz, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.