메뉴 건너뛰기




Volumn 8, Issue 7, 2009, Pages 933-943

Photophysics and photochemistry of rose bengal bound to human serum albumin

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; ROSE BENGAL;

EID: 68149158138     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b901056d     Document Type: Article
Times cited : (70)

References (61)
  • 1
    • 0021111937 scopus 로고
    • Singlet oxygen production by lactoperoxidase
    • J. R. Kanofsky Singlet oxygen production by lactoperoxidase J. Biol. Chem. 1983 258 5991 5993
    • (1983) J. Biol. Chem. , vol.258 , pp. 5991-5993
    • Kanofsky, J.R.1
  • 2
    • 0021352686 scopus 로고
    • Singlet oxygen production by chloroperoxidase-hydrogen peroxide-halide systems
    • J. R. Kanofsky Singlet oxygen production by chloroperoxidase-hydrogen peroxide-halide systems J. Biol. Chem. 1984 259 5596 5600
    • (1984) J. Biol. Chem. , vol.259 , pp. 5596-5600
    • Kanofsky, J.R.1
  • 3
    • 0021750194 scopus 로고
    • Biochemical requirements for singlet oxygen production by purified human myeloperoxidase
    • J. R. Kanofsky J. Wright G. E. Miles-Richardson A. I. Tauber Biochemical requirements for singlet oxygen production by purified human myeloperoxidase J. Clin. Invest. 1984 74 1489 1495
    • (1984) J. Clin. Invest. , vol.74 , pp. 1489-1495
    • Kanofsky, J.R.1    Wright, J.2    Miles-Richardson, G.E.3    Tauber, A.I.4
  • 5
    • 0027185676 scopus 로고
    • Extra cellular production of singlet oxygen by stimulated macrophages quantified using 9,10-diphenylanthracene and peryline in a polystyrene film
    • M. J. Steinbeck A. U. Khan M. J. Kanjorski Extra cellular production of singlet oxygen by stimulated macrophages quantified using 9,10- diphenylanthracene and peryline in a polystyrene film J. Biol. Chem. 1993 268 15649 15654
    • (1993) J. Biol. Chem. , vol.268 , pp. 15649-15654
    • Steinbeck, M.J.1    Khan, A.U.2    Kanjorski, M.J.3
  • 6
    • 0033937772 scopus 로고    scopus 로고
    • Photosensitized production of singlet oxygen
    • I. E. Kochevar R. W. Redmond Photosensitized production of singlet oxygen Methods Enzymol. 2000 319 20 28
    • (2000) Methods Enzymol. , vol.319 , pp. 20-28
    • Kochevar, I.E.1    Redmond, R.W.2
  • 7
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and proteins damage
    • M. J. Davies The oxidative environment and proteins damage Biochim. Biophys. Acta 2005 1703 93 109
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 8
    • 0037564169 scopus 로고    scopus 로고
    • Singlet oxygen-mediated damage to proteins and its consequences
    • M. J. Davies Singlet oxygen-mediated damage to proteins and its consequences Biochem. Biophys. Res. Commun. 2003 305 761 770
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 761-770
    • Davies, M.J.1
  • 9
    • 0034696781 scopus 로고    scopus 로고
    • Protein degradation by peroxide catalyzed by chromium (III): Role of coordinated ligand
    • H. Y. Shrivastava B. U. Nair Protein degradation by peroxide catalyzed by chromium (III): Role of coordinated ligand Biochem. Biophys. Res. Commun. 2000 270 749 754
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 749-754
    • Shrivastava, H.Y.1    Nair, B.U.2
  • 10
    • 0022393446 scopus 로고
    • Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron
    • K. Kim S. G. Rhee E. R. Stadtman Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron J. Biol. Chem. 1985 260 15394 15397
    • (1985) J. Biol. Chem. , vol.260 , pp. 15394-15397
    • Kim, K.1    Rhee, S.G.2    Stadtman, E.R.3
  • 11
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • E. R. Stadtman B. S. Berlett Reactive oxygen-mediated protein oxidation in aging and disease Chem. Res. Toxicol. 1997 10 485 494
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 12
    • 0036632772 scopus 로고    scopus 로고
    • Singlet oxygen-mediated protein oxidation: Evidence for the formation of reactive side chain peroxides on tyrosine residues
    • A. Wright W. A. Bubb C. L. Hawkins M. J. Davies Singlet oxygen-mediated protein oxidation: evidence for the formation of reactive side chain peroxides on tyrosine residues Photochem. Photobiol. 2002 76 35 46
    • (2002) Photochem. Photobiol. , vol.76 , pp. 35-46
    • Wright, A.1    Bubb, W.A.2    Hawkins, C.L.3    Davies, M.J.4
  • 13
    • 85047695047 scopus 로고    scopus 로고
    • Inhibition of glyceraldehyde-3-phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack
    • P. E. Morgan R. T. Dean M. J. Davies Inhibition of glyceraldehyde-3- phosphate dehydrogenase by peptide and protein peroxides generated by singlet oxygen attack Eur. J. Biochem. 2002 269 1916 1925
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1916-1925
    • Morgan, P.E.1    Dean, R.T.2    Davies, M.J.3
  • 14
    • 34247127332 scopus 로고    scopus 로고
    • Inhibition of protein tyrosine phosphatases by amino acid, peptide, and protein hydroperoxides: Potential modulation of cell signaling by protein oxidation products
    • M. Gracanin M. J. Davies Inhibition of protein tyrosine phosphatases by amino acid, peptide, and protein hydroperoxides: potential modulation of cell signaling by protein oxidation products Free Radical Biol. Med. 2007 42 1543 51
    • (2007) Free Radical Biol. Med. , vol.42 , pp. 1543-1551
    • Gracanin, M.1    Davies, M.J.2
  • 15
    • 0037443717 scopus 로고    scopus 로고
    • Photo-oxidation of cells generates long-lived intracellular protein peroxides
    • A. Wright C. L. Hawkins M. J. Davies Photo-oxidation of cells generates long-lived intracellular protein peroxides Free Radical Biol. Med. 2003 34 637 647
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 637-647
    • Wright, A.1    Hawkins, C.L.2    Davies, M.J.3
  • 16
    • 1242298607 scopus 로고    scopus 로고
    • Protective mechanisms against peptide and protein peroxides generated by singlet oxygen
    • P. E. Morgan R. T. Dean M. J. Davies Protective mechanisms against peptide and protein peroxides generated by singlet oxygen Free Radical Biol. Med. 2004 36 484 496
    • (2004) Free Radical Biol. Med. , vol.36 , pp. 484-496
    • Morgan, P.E.1    Dean, R.T.2    Davies, M.J.3
  • 19
    • 0041906767 scopus 로고
    • Picosecond studies of rose bengal fluorescence in reverse micellar systems
    • Ed. Plenum Press, New York
    • M. A. J. Rodgerd, Picosecond studies of rose bengal fluorescence in reverse micellar systems. In Reverse Micelles, Ed. Plenum Press, New York, 1984, pp 164-173
    • (1984) Reverse Micelles , pp. 164-173
    • Rodgerd, M.A.J.1
  • 20
    • 0001028296 scopus 로고
    • Picosecond fluorescence studies of rose bengal in aqueous micellar dispersions
    • M. A. J. Rodgerd Picosecond fluorescence studies of rose bengal in aqueous micellar dispersions Chem. Phys. Lett. 1981 78 509 514
    • (1981) Chem. Phys. Lett. , vol.78 , pp. 509-514
    • Rodgerd, M.A.J.1
  • 21
    • 0000284451 scopus 로고
    • Influence of cationic surfactant on the photoprocesses of eosine and rose bengal in aqueous solution
    • P. Bliski R. Dabestani C. F. Chingnell Influence of cationic surfactant on the photoprocesses of eosine and rose bengal in aqueous solution J. Phys. Chem. 1991 95 5784 5791
    • (1991) J. Phys. Chem. , vol.95 , pp. 5784-5791
    • Bliski, P.1    Dabestani, R.2    Chingnell, C.F.3
  • 23
    • 33947093673 scopus 로고
    • Hydrogen bond strengths from solvent dependence lifetimes of rose bengal dye
    • L. E. Cramer K. G. Spears Hydrogen bond strengths from solvent dependence lifetimes of rose bengal dye J. Am. Chem. Soc. 1978 100 221 227
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 221-227
    • Cramer, L.E.1    Spears, K.G.2
  • 24
  • 25
    • 0001760657 scopus 로고
    • Solubility and propiertes of Eosin y and rose bengal triplet state in sodium docecyl sulfate micellar solutios
    • A. Seret A. Van de Vorts Solubility and propiertes of Eosin Y and rose bengal triplet state in sodium docecyl sulfate micellar solutios J. Phys. Chem. 1990 94 5293 5299
    • (1990) J. Phys. Chem. , vol.94 , pp. 5293-5299
    • Seret, A.1    Van De Vorts, A.2
  • 26
    • 0002668561 scopus 로고    scopus 로고
    • Solvent effect on rates of photochemical reactions of rose bengal triplet state studied by nanosecond laser flash photolysis
    • S. D.-M. Islam O. Ito Solvent effect on rates of photochemical reactions of rose bengal triplet state studied by nanosecond laser flash photolysis J. Photochem. Photobiol., A 1999 123 53 59
    • (1999) J. Photochem. Photobiol., A , vol.123 , pp. 53-59
    • Islam, S.D.-M.1    Ito, O.2
  • 27
    • 0003626648 scopus 로고    scopus 로고
    • Academic press, New York, first edn., ch. 3
    • T. Peters, All about albumin proteins. Academic press, New York, first edn., 1996, ch. 3
    • (1996) All about Albumin Proteins
    • Peters, T.1
  • 28
    • 0034039993 scopus 로고    scopus 로고
    • Ligand binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands
    • F. A. De Wolf G. M. Brett Ligand binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands Pharmacol. Rev. 2000 52 200 236
    • (2000) Pharmacol. Rev. , vol.52 , pp. 200-236
    • De Wolf, F.A.1    Brett, G.M.2
  • 29
    • 0025378934 scopus 로고
    • Structure and ligand binding properties of human serum albumin (Review)
    • U. Kragh-Hansen Structure and ligand binding properties of human serum albumin (Review) Dan. Med. Bull. 1990 37 57 84
    • (1990) Dan. Med. Bull. , vol.37 , pp. 57-84
    • Kragh-Hansen, U.1
  • 30
    • 0025322080 scopus 로고
    • Conformational changes in human serum albumin induced by ligand binding
    • B. Honoré Conformational changes in human serum albumin induced by ligand binding Phamacol. Toxicol. 1990 66 7 26
    • (1990) Phamacol. Toxicol. , vol.66 , pp. 7-26
    • Honoré, B.1
  • 31
    • 0027408611 scopus 로고
    • Quantitative analyses of the interaction between calcium ions and human serum albumin
    • U. Kragh-Hansen H. Vorum Quantitative analyses of the interaction between calcium ions and human serum albumin Clin. Chem. 1993 39 202 208
    • (1993) Clin. Chem. , vol.39 , pp. 202-208
    • Kragh-Hansen, U.1    Vorum, H.2
  • 32
    • 37749047471 scopus 로고    scopus 로고
    • Identification of high affinity fatty acid binding sites on human serum albumin by MM-PBSA method
    • S. I. Fujiwara T. Amisaki Identification of high affinity fatty acid binding sites on human serum albumin by MM-PBSA method J. Biophys. 2008 94 95 103
    • (2008) J. Biophys. , vol.94 , pp. 95-103
    • Fujiwara, S.I.1    Amisaki, T.2
  • 33
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X. M. He D. C. Carter Atomic structure and chemistry of human serum albumin Nature. 1992 358 209 215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 34
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • G. Sudlow D. J. Birkett D. N. Wade The characterization of two specific drug binding sites on human serum albumin Mol. Pharmacol. 1975 11 824 832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 35
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • G. Sudlow D. J. Birkett D. N. Wade Further characterization of specific drug binding sites on human serum albumin Mol. Pharmacol. 1976 12 1052 1061
    • (1976) Mol. Pharmacol. , vol.12 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 36
    • 0033842504 scopus 로고    scopus 로고
    • Five recombinant fragments of human serum albumin-Tools for the characterization of the warfarin binding site
    • M. Dockal M. Chang D. C. Carter F. Ruker Five recombinant fragments of human serum albumin-Tools for the characterization of the warfarin binding site Protein Sci. 2000 9 1455 1465
    • (2000) Protein Sci. , vol.9 , pp. 1455-1465
    • Dockal, M.1    Chang, M.2    Carter, D.C.3    Ruker, F.4
  • 37
    • 0028989459 scopus 로고
    • A general, wide-rage spectrofluorometric method for measuring the site-specific affinities of drugs toward human serum albumin
    • D. E. Epps T. J. Raub F. J. Kézdy A general, wide-rage spectrofluorometric method for measuring the site-specific affinities of drugs toward human serum albumin Anal. Biochem. 1995 227 342 350
    • (1995) Anal. Biochem. , vol.227 , pp. 342-350
    • Epps, D.E.1    Raub, T.J.2    Kézdy, F.J.3
  • 38
    • 0033054548 scopus 로고    scopus 로고
    • Determination of the affinity of the drugs toward serum albumin by measurement of the quenching of the intrinsic tryptophan fluorescent of the protein
    • D. E. Epps T. J. Raub V. Caiolfa A. Chari M. Zamai Determination of the affinity of the drugs toward serum albumin by measurement of the quenching of the intrinsic tryptophan fluorescent of the protein J. Pharm. Pharmacol. 1998 51 41 48
    • (1998) J. Pharm. Pharmacol. , vol.51 , pp. 41-48
    • Epps, D.E.1    Raub, T.J.2    Caiolfa, V.3    Chari, A.4    Zamai, M.5
  • 39
    • 34547322005 scopus 로고    scopus 로고
    • Determination of drug-serum protein interactions via fluorescence polarization measurements
    • U. Mathias M. Jung Determination of drug-serum protein interactions via fluorescence polarization measurements Anal. Bimanual. Chem. 2007 388 1147 1156
    • (2007) Anal. Bimanual. Chem. , vol.388 , pp. 1147-1156
    • Mathias, U.1    Jung, M.2
  • 40
    • 34547093163 scopus 로고    scopus 로고
    • Characterization of the myricetin-human serum albumin complex by spectroscopic and molecular modeling approaches
    • C. Qin M. X. Xie Y. Liu Characterization of the myricetin-human serum albumin complex by spectroscopic and molecular modeling approaches Biomacromolecules 2007 8 2182 2189
    • (2007) Biomacromolecules , vol.8 , pp. 2182-2189
    • Qin, C.1    Xie, M.X.2    Liu, Y.3
  • 41
    • 34548138940 scopus 로고    scopus 로고
    • Modulation of heme and myristate binding to human serum albumin by anti-HIV drugs, An optical and NMR spectroscopic study
    • G. Fanali A. Bocedi P. Ascenzi M. Fasano Modulation of heme and myristate binding to human serum albumin by anti-HIV drugs, An optical and NMR spectroscopic study FEBS J. 2007 274 4491 4502
    • (2007) FEBS J. , vol.274 , pp. 4491-4502
    • Fanali, G.1    Bocedi, A.2    Ascenzi, P.3    Fasano, M.4
  • 42
    • 0345328130 scopus 로고    scopus 로고
    • Photophysical studies on binding of curcumin to bovine serum albumins
    • A. Barik K. I. Priyadarsini H. Mohan Photophysical studies on binding of curcumin to bovine serum albumins Photochem. Photobiol. 2003 77 597 603
    • (2003) Photochem. Photobiol. , vol.77 , pp. 597-603
    • Barik, A.1    Priyadarsini, K.I.2    Mohan, H.3
  • 43
    • 0019937203 scopus 로고
    • Effect of albumin binding on the hepatic transport of rose bengal: Surface-Mediated dissociation of limited capacity
    • E. L. Forker B. A. Luxon M. Snell W. O. Shurmantine Effect of albumin binding on the hepatic transport of rose bengal: Surface-Mediated dissociation of limited capacity J. Pharmacol. Exp. Ther. 1982 223 342 347
    • (1982) J. Pharmacol. Exp. Ther. , vol.223 , pp. 342-347
    • Forker, E.L.1    Luxon, B.A.2    Snell, M.3    Shurmantine, W.O.4
  • 44
    • 0021029231 scopus 로고
    • Albumin-mediated transport of rose bengal by perfused rat liver: Kinetics of the reaction at cell surface
    • E. L. Forker B. A. Luxon Albumin-mediated transport of rose bengal by perfused rat liver: Kinetics of the reaction at cell surface J. Clin. Invest. 1983 72 1764 1771
    • (1983) J. Clin. Invest. , vol.72 , pp. 1764-1771
    • Forker, E.L.1    Luxon, B.A.2
  • 46
    • 84981611610 scopus 로고
    • The fluorescence of native, denaturated and reduced-denaturated proteins
    • M. J. Kronman L. G. Holmes The fluorescence of native, denaturated and reduced-denaturated proteins Photochem. Photobiol. 1971 14 113 134
    • (1971) Photochem. Photobiol. , vol.14 , pp. 113-134
    • Kronman, M.J.1    Holmes, L.G.2
  • 47
    • 37049080392 scopus 로고
    • Experimental correction for the inner-filter effect in fluorescence spectra
    • M. Kubista R. Sojback S. Ericksson B. Albinsson Experimental correction for the inner-filter effect in fluorescence spectra Analyst 1994 119 417 419
    • (1994) Analyst , vol.119 , pp. 417-419
    • Kubista, M.1    Sojback, R.2    Ericksson, S.3    Albinsson, B.4
  • 49
    • 34047225838 scopus 로고    scopus 로고
    • Photoprotection of vitamins in skimmed milk by aqueous soluble lycopene-gum arabic microcapsule
    • M. A. Montenegro I. L. Nunes A. Z. Mercadante C. D. Borsarelli Photoprotection of vitamins in skimmed milk by aqueous soluble lycopene-gum arabic microcapsule J. Agric. Food Chem. 2007 55 323 329
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 323-329
    • Montenegro, M.A.1    Nunes, I.L.2    Mercadante, A.Z.3    Borsarelli, C.D.4
  • 51
    • 0019508807 scopus 로고
    • Improved techniques for the separation of serum lipoproteins by density gradient ultracentrifugation: Visualization by prestaining and rapid separation of serum lipoproteins from small volumes of serum
    • A. H. Terpstra C. J. Woodward F. J. Sanchez-Muniz Improved techniques for the separation of serum lipoproteins by density gradient ultracentrifugation: visualization by prestaining and rapid separation of serum lipoproteins from small volumes of serum Anal. Biochem. 1981 111 149 157
    • (1981) Anal. Biochem. , vol.111 , pp. 149-157
    • Terpstra, A.H.1    Woodward, C.J.2    Sanchez-Muniz, F.J.3
  • 52
    • 49049139427 scopus 로고
    • Evaluation of partition constant in compartmentalized systems from fluorescence quenching data
    • M. V. Encinas E. Lissi Evaluation of partition constant in compartmentalized systems from fluorescence quenching data Chem. Phys. Lett. 1982 91 55 57
    • (1982) Chem. Phys. Lett. , vol.91 , pp. 55-57
    • Encinas, M.V.1    Lissi, E.2
  • 53
    • 0014210820 scopus 로고
    • Fluorescence decay times: Proteins, coenzymes, and other compounds in water
    • F. R. Chen. Raymond G. G. Vurek N. Alexander Fluorescence Decay Times: Proteins, Coenzymes, and Other Compounds in Water Science 1967 156 949 951
    • (1967) Science , vol.156 , pp. 949-951
    • Chen, F.R.1    Raymond, G.2    Vurek, G.3    Alexander, N.4
  • 54
    • 0030198728 scopus 로고    scopus 로고
    • Study of photoinduced energy and electron transfer in α-terthienyl-bovine serum albumin conjugates: A laser flash photolysis study
    • R. Boch N. Mohtat Y. Lear J. T. Arnason T. Durst J. C. Scaiano Study of photoinduced energy and electron transfer in α-terthienyl-bovine serum albumin conjugates: a laser flash photolysis study Photochem. Photobiol. 1996 64 92 99
    • (1996) Photochem. Photobiol. , vol.64 , pp. 92-99
    • Boch, R.1    Mohtat, N.2    Lear, Y.3    Arnason, J.T.4    Durst, T.5    Scaiano, J.C.6
  • 55
    • 0010593040 scopus 로고
    • Diffusion and concentration of oxygen in microheterogeneous systems, Evaluation from luminescence quenching data
    • E. B. Abuin E. A. Lissi Diffusion and concentration of oxygen in microheterogeneous systems, Evaluation from luminescence quenching data Prog. Reaction Kinetics. 1991 16 1 33
    • (1991) Prog. Reaction Kinetics. , vol.16 , pp. 1-33
    • Abuin, E.B.1    Lissi, E.A.2
  • 56
    • 0024372896 scopus 로고
    • Oxygen diffusion-concentration in erythrocyte plasma membranes studied by the fluorescence quenching of anionic and cationic pyrene derivatives
    • E. A. Lissi T. Caceres Oxygen diffusion-concentration in erythrocyte plasma membranes studied by the fluorescence quenching of anionic and cationic pyrene derivatives J. Bioenerg. Biomembr. 1989 21 375 385
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 375-385
    • Lissi, E.A.1    Caceres, T.2
  • 57
    • 0036726196 scopus 로고    scopus 로고
    • Photobleaching of Hypericin bound to Human serum albumin, cultured adenocarcinoma cells and nude mice skin
    • A. B. Uzdensky V. Iani L.-W. Ma J. Moan Photobleaching of Hypericin bound to Human serum albumin, cultured adenocarcinoma cells and nude mice skin Photochem. Photobiol. 2002 76 320 328
    • (2002) Photochem. Photobiol. , vol.76 , pp. 320-328
    • Uzdensky, A.B.1    Iani, V.2    Ma, L.-W.3    Moan, J.4
  • 58
    • 84985433662 scopus 로고
    • Spectral characteristics and mechanisms of chemiluminiscence from tryptophan solutions induced by UV-Irradiation
    • J. Slawinski M. Elbanowski D. Slawinska Spectral Characteristics and mechanisms of chemiluminiscence from tryptophan solutions induced by UV-Irradiation Photochem. Photobiol. 1980 32 253 260
    • (1980) Photochem. Photobiol. , vol.32 , pp. 253-260
    • Slawinski, J.1    Elbanowski, M.2    Slawinska, D.3
  • 59
    • 0025104818 scopus 로고
    • Photoreactions of macrocyclic dyes bound to human serum albumin
    • J. Davila A. Harriman Photoreactions of macrocyclic dyes bound to human serum albumin Photochem. Photobiol. 1990 51 9 19
    • (1990) Photochem. Photobiol. , vol.51 , pp. 9-19
    • Davila, J.1    Harriman, A.2
  • 61
    • 44849108936 scopus 로고    scopus 로고
    • Autosensitized oxidation of glycated bovine lens proteins irradiated with UVA-visible light at low oxygen concentration
    • F. Avila A. Matus D. Fuentealba E. Lissi B. Friguet E. Silva Autosensitized oxidation of glycated bovine lens proteins irradiated with UVA-visible light at low oxygen concentration Photochem. Photobiol. Sci. 2008 7 718 24
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 718-724
    • Avila, F.1    Matus, A.2    Fuentealba, D.3    Lissi, E.4    Friguet, B.5    Silva, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.