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Volumn 63, Issue 6, 1996, Pages 762-767

Development of monoclonal antibodies against a riboflavin-tryptophan photoinduced adduct: Reactivity to eye lens proteins

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE;

EID: 0030156340     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1996.tb09628.x     Document Type: Conference Paper
Times cited : (13)

References (49)
  • 1
    • 0020019560 scopus 로고
    • Serum sulfated lithocholate as an indicator of cholestasis during parenteral nutrition in infants and children
    • Parrel, M. K., W. F. Balistreri and F. J. Suchy (1982) Serum sulfated lithocholate as an indicator of cholestasis during parenteral nutrition in infants and children. J. Parenter. Enteral Nutr. 6, 30-33.
    • (1982) J. Parenter. Enteral Nutr. , vol.6 , pp. 30-33
    • Parrel, M.K.1    Balistreri, W.F.2    Suchy, F.J.3
  • 3
    • 0016699299 scopus 로고
    • Lethal effect of "daylight" fluorescent light on human cells in tissue-culture medium
    • Wang, R. J. (1975) Lethal effect of "daylight" fluorescent light on human cells in tissue-culture medium. Photockem. Photobiol. 21, 373-375.
    • (1975) Photockem. Photobiol. , vol.21 , pp. 373-375
    • Wang, R.J.1
  • 4
    • 0017702119 scopus 로고
    • Formation of photoproducts lethal for human cells in culture by daylight fluorescent light and bilirubin light
    • Nixon, R. T. and R. J. Wang (1977) Formation of photoproducts lethal for human cells in culture by daylight fluorescent light and bilirubin light. Photochem. Photobiol. 26, 589-593.
    • (1977) Photochem. Photobiol. , vol.26 , pp. 589-593
    • Nixon, R.T.1    Wang, R.J.2
  • 6
    • 0023914317 scopus 로고
    • Tryptophan riboflavin photo-induced adduct and hepatic dysfunction in rats
    • Donoso, M. N., A. Valenzuela and E. Silva (1988) Tryptophan riboflavin photo-induced adduct and hepatic dysfunction in rats. Nutr. Rep. Int 37, 599-606.
    • (1988) Nutr. Rep. Int , vol.37 , pp. 599-606
    • Donoso, M.N.1    Valenzuela, A.2    Silva, E.3
  • 7
    • 0024272345 scopus 로고
    • Toxic effect of a photo-induced tryptophan-riboflavin adduct on F9 teratocarcinoma cells and preimplantation mouse embryos
    • Silva, E., M. Salim-Hanna, M. I. Becker and A. E. De Ioannes (1988) Toxic effect of a photo-induced tryptophan-riboflavin adduct on F9 teratocarcinoma cells and preimplantation mouse embryos. Int. J. Vitam. Nutr. Res. 58, 394-401.
    • (1988) Int. J. Vitam. Nutr. Res. , vol.58 , pp. 394-401
    • Silva, E.1    Salim-Hanna, M.2    Becker, M.I.3    De Ioannes, A.E.4
  • 8
  • 9
    • 0027228162 scopus 로고
    • Photochemically induced cataracts in rat lenses can be prevented by AL-3823 A, a glutathione peroxidase mimic
    • Spector, A., G.-M. Wang and R.-R. Wang (1993) Photochemically induced cataracts in rat lenses can be prevented by AL-3823 A, a glutathione peroxidase mimic. Proc. Natl. Acad. Sci. USA 90, 7485-7489.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7485-7489
    • Spector, A.1    Wang, G.-M.2    Wang, R.-R.3
  • 11
    • 0027717456 scopus 로고
    • The prevention of cataract caused by oxidative stress in cultured rat lenses. II. Early effects of photochemical stress and recovery
    • Spector, A., G.-M. Wang and R.-R. Wang (1993) The prevention of cataract caused by oxidative stress in cultured rat lenses. II. Early effects of photochemical stress and recovery Exp Eye Res. 57, 659-667.
    • (1993) Exp Eye Res. , vol.57 , pp. 659-667
    • Spector, A.1    Wang, G.-M.2    Wang, R.-R.3
  • 12
    • 0019573907 scopus 로고
    • Photosensitized oxidatión in the ocular lens: Evidence for photsensitizers endogenous to the human lens
    • Zigler, J. S., Jr. and J. D. Goosey (1981) Photosensitized oxidatión in the ocular lens: evidence for photsensitizers endogenous to the human lens. Photochem. Photobiol. 33, 869-874.
    • (1981) Photochem. Photobiol. , vol.33 , pp. 869-874
    • Zigler Jr., J.S.1    Goosey, J.D.2
  • 13
    • 0242341773 scopus 로고
    • Aging of protein molecules: Lens crystallins as a model system
    • Zigler, J. S., Jr and J. D. Goosey (1981) Aging of protein molecules: lens crystallins as a model system. Trends Biochem. Sci. 6, 133-136.
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 133-136
    • Zigler Jr., J.S.1    Goosey, J.D.2
  • 14
    • 0029067323 scopus 로고
    • A brief photochemically induced oxidative insult causes irreversible lens damage and cataract I. Transparency and epithelial cell layer
    • Spector, A., G.-M. Wang, R.-R. Wang, W.-C. Li and J. R. Kuszak (1995) A brief photochemically induced oxidative insult causes irreversible lens damage and cataract I. Transparency and epithelial cell layer. Exp. Eye Res. 60, 471-481.
    • (1995) Exp. Eye Res. , vol.60 , pp. 471-481
    • Spector, A.1    Wang, G.-M.2    Wang, R.-R.3    Li, W.-C.4    Kuszak, J.R.5
  • 15
    • 0029042937 scopus 로고
    • A brief photochemically induced oxidative insult causes irreversible lens damage and cataract II. Mechamisn of action
    • Spector, A., G.-M. Wang, R.-R. Wang, W.-C. Li and N. J. Kleiman (1995) A brief photochemically induced oxidative insult causes irreversible lens damage and cataract II. Mechamisn of action. Exp. Eye Res. 60, 483-493.
    • (1995) Exp. Eye Res. , vol.60 , pp. 483-493
    • Spector, A.1    Wang, G.-M.2    Wang, R.-R.3    Li, W.-C.4    Kleiman, N.J.5
  • 16
    • 0026522281 scopus 로고
    • Anaerobic riboflavin photosensitized modification of rat lens proteins. A correlation with aged-related changes
    • Ugarte, R., A. M. Edwards, M. S. Diez, A. Valenzuela and E. Silva (1992) Anaerobic riboflavin photosensitized modification of rat lens proteins. A correlation with aged-related changes. J. Photochem. Photobiol. B Biol. 13, 161-168.
    • (1992) J. Photochem. Photobiol. B Biol. , vol.13 , pp. 161-168
    • Ugarte, R.1    Edwards, A.M.2    Diez, M.S.3    Valenzuela, A.4    Silva, E.5
  • 17
    • 0024117783 scopus 로고
    • Lumiflavin-sensitized photooxygenation of indole
    • Yoshimura, A. and T. Ohno (1988) Lumiflavin-sensitized photooxygenation of indole Photochem. Photobiol. 48, 561-565.
    • (1988) Photochem. Photobiol. , vol.48 , pp. 561-565
    • Yoshimura, A.1    Ohno, T.2
  • 19
    • 0017732708 scopus 로고
    • Light-induced binding of riboflavin to lysozyme
    • Silva, E. and J. Gaule (1977) Light-induced binding of riboflavin to lysozyme. Radiat. Environ. Biophys. 14, 303-310.
    • (1977) Radiat. Environ. Biophys. , vol.14 , pp. 303-310
    • Silva, E.1    Gaule, J.2
  • 20
    • 0021971922 scopus 로고
    • Study of a photo-induced lysozyme-riboflavin bond
    • Ferrer, I. and E. Silva (1985) Study of a photo-induced lysozyme-riboflavin bond. Radiat. Environ. Biophys. 24, 63-70.
    • (1985) Radiat. Environ. Biophys. , vol.24 , pp. 63-70
    • Ferrer, I.1    Silva, E.2
  • 21
    • 0020711918 scopus 로고
    • Binding of riboflavin to lysozyme promoted by peroxidase-generated triplet acetone
    • Durán, N., M. Haun, S. M. De Toledo, G. Cilento and E. Silva (1983) Binding of riboflavin to lysozyme promoted by peroxidase-generated triplet acetone. Photochem. Photobiol. 37, 247-250.
    • (1983) Photochem. Photobiol. , vol.37 , pp. 247-250
    • Durán, N.1    Haun, M.2    De Toledo, S.M.3    Cilento, G.4    Silva, E.5
  • 22
    • 0023970150 scopus 로고
    • Photochemical-like behaviour of riboflavin in the dark promoted by enzyme-generated triplet acetone
    • Rojas, J. and E. Silva (1988) Photochemical-like behaviour of riboflavin in the dark promoted by enzyme-generated triplet acetone. Photochem. Photobiol. 47, 467-470.
    • (1988) Photochem. Photobiol. , vol.47 , pp. 467-470
    • Rojas, J.1    Silva, E.2
  • 23
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells
    • Köhler, G. and C. Milstein (1975) Continuous cultures of fused cells. Nature 256, 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 86, 142-146.
    • (1976) Anal. Biochem. , vol.86 , pp. 142-146
    • Bradford, M.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0018872277 scopus 로고
    • Detection of antibodies against foot- and mouth-disease virus using purified staphylococcus. A protein conjugated with alkaline phosphatase
    • Crowther, J. R. and E. M. E. Abu-Elzeein (1980) Detection of antibodies against foot- and mouth-disease virus using purified staphylococcus. A protein conjugated with alkaline phosphatase. J. Immunol. Methods 34, 261.
    • (1980) J. Immunol. Methods , vol.34 , pp. 261
    • Crowther, J.R.1    Abu-Elzeein, E.M.E.2
  • 27
    • 0028603564 scopus 로고
    • Development of anti-human B blood group monoclonal antibodies suitable as a blood typing reagent
    • Becker, M. I., F. Juica, A. Jamett, S. Tzichinovsky, S. Barros, J. Aguayo and A. De Ioannes (1994) Development of anti-human B blood group monoclonal antibodies suitable as a blood typing reagent. Hybridoma 13, 303-310.
    • (1994) Hybridoma , vol.13 , pp. 303-310
    • Becker, M.I.1    Juica, F.2    Jamett, A.3    Tzichinovsky, S.4    Barros, S.5    Aguayo, J.6    De Ioannes, A.7
  • 30
    • 0026574643 scopus 로고
    • Preparation of monoclonal mouse antibodies against two specific eumelanin related compounds
    • Kammeyer, A., L. A. Oomen and S. Pavel (1992) Preparation of monoclonal mouse antibodies against two specific eumelanin related compounds. J. Immunol. Methods 156, 61-67.
    • (1992) J. Immunol. Methods , vol.156 , pp. 61-67
    • Kammeyer, A.1    Oomen, L.A.2    Pavel, S.3
  • 31
    • 0026101290 scopus 로고
    • Photoinduced riboflavin binding to the tryptophan residues of bovine and human serum albumins
    • Tapia, G. and E. Silva (1991) Photoinduced riboflavin binding to the tryptophan residues of bovine and human serum albumins. Radiat. Environ. Biophys. 30, 131-138.
    • (1991) Radiat. Environ. Biophys. , vol.30 , pp. 131-138
    • Tapia, G.1    Silva, E.2
  • 32
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residsues in protein molecules
    • Burstein, E. A., N. S. Vedenkina and M. N. Ivkova (1973) Fluorescence and the location of tryptophan residsues in protein molecules. Photochem. Photobiol. 18, 263-279.
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 33
    • 0022527517 scopus 로고
    • Exposure of tryptophanyl residues in α-lactalbumin and lysozyme. Quantitative determination by fluorescence quenching studies
    • Edwards, A. M. and E. Silva (1986) Exposure of tryptophanyl residues in α-lactalbumin and lysozyme. Quantitative determination by fluorescence quenching studies. Radiat. Environ. Biophys. 25, 113-122.
    • (1986) Radiat. Environ. Biophys. , vol.25 , pp. 113-122
    • Edwards, A.M.1    Silva, E.2
  • 34
    • 0023813177 scopus 로고
    • Age-related increase in concentration and aggregation of degraded polypeptides in human lenses
    • Srivastava, O. P. (1988) Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp. Eye Res. 47, 525-543.
    • (1988) Exp. Eye Res. , vol.47 , pp. 525-543
    • Srivastava, O.P.1
  • 35
    • 0024585808 scopus 로고
    • The effects of aging and cataract formation on the trypsin inhibitor activity of human lens
    • Srivastava, O. P. and B. J. Ortwerth (1989) The effects of aging and cataract formation on the trypsin inhibitor activity of human lens. Exp. Eye Res. 48, 25-36.
    • (1989) Exp. Eye Res. , vol.48 , pp. 25-36
    • Srivastava, O.P.1    Ortwerth, B.J.2
  • 36
    • 0026563022 scopus 로고
    • A possible biological role of the electron transfer between tyrosine and tryptophan
    • Lee, C. Y. (1992) A possible biological role of the electron transfer between tyrosine and tryptophan. FEBS Lett 299, 119-123.
    • (1992) FEBS Lett , vol.299 , pp. 119-123
    • Lee, C.Y.1
  • 37
    • 0019129187 scopus 로고
    • A comparison of aerobic and anaerobic photolysis of lens protein
    • Dillon, J. and A. Spector (1980) A comparison of aerobic and anaerobic photolysis of lens protein. Exp. Eve Res. 31, 591-599.
    • (1980) Exp. Eve Res. , vol.31 , pp. 591-599
    • Dillon, J.1    Spector, A.2
  • 38
    • 0025001969 scopus 로고
    • Comparison of effects of L-tryptophan and a tryptophan analog, D,L-β-(1-naphtyl) alanine, on processes relating to hepatic proteins synthesis in rats
    • Sidransky, H., E. Verney and R. Kurl (1990) Comparison of effects of L-tryptophan and a tryptophan analog, D,L-β-(1-naphtyl) alanine, on processes relating to hepatic proteins synthesis in rats. J. Nutr. 120, 1157-1162.
    • (1990) J. Nutr. , vol.120 , pp. 1157-1162
    • Sidransky, H.1    Verney, E.2    Kurl, R.3
  • 39
    • 0026694058 scopus 로고
    • Studies with compounds that compete with tryptophan binding to rat hepatic nuclei
    • Sidransky, H., E. Verney, J. W. Cosgrove and A. Schwartz (1992) Studies with compounds that compete with tryptophan binding to rat hepatic nuclei. J. Nutr. 122, 1085-1095.
    • (1992) J. Nutr. , vol.122 , pp. 1085-1095
    • Sidransky, H.1    Verney, E.2    Cosgrove, J.W.3    Schwartz, A.4
  • 40
    • 0026453024 scopus 로고
    • Competitive studies relating to tryptophan binding to hepatic nuclear envelopes as a sensitive assay for unknown compounds
    • Sidransky, H., E. Verney and J. W. Cosgrove (1992) Competitive studies relating to tryptophan binding to hepatic nuclear envelopes as a sensitive assay for unknown compounds. Toxicology 76, 89-100.
    • (1992) Toxicology , vol.76 , pp. 89-100
    • Sidransky, H.1    Verney, E.2    Cosgrove, J.W.3
  • 42
    • 0026063268 scopus 로고
    • Sequence-dependent interaction of acidic aminoacid with guanine base in tryptophan-containing dipeptides: Spectroscopic studies
    • Igo, H., H. Ueda, Y. Usami, Y. Kafuku, M. Doi, M. Inoue and T. Ishida (1991) Sequence-dependent interaction of acidic aminoacid with guanine base in tryptophan-containing dipeptides: spectroscopic studies. Chem. Pharm. Bull. 39, 2483-2486.
    • (1991) Chem. Pharm. Bull. , vol.39 , pp. 2483-2486
    • Igo, H.1    Ueda, H.2    Usami, Y.3    Kafuku, Y.4    Doi, M.5    Inoue, M.6    Ishida, T.7
  • 45
    • 0026608615 scopus 로고
    • Mutual assistance of hydrogen-bond pairing and aromatic stacking interactions for molecular recognition spectroscopic study on the interaction of guanine base with cytosine and tryptophan molecules
    • Tarni, M , H. Furumura, Y. Kafuku, T. Ishida and M. Inoue (1992) Mutual assistance of hydrogen-bond pairing and aromatic stacking interactions for molecular recognition spectroscopic study on the interaction of guanine base with cytosine and tryptophan molecules. Biochem. Biophys. Res. Commun. 183, 577-583.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 577-583
    • Tarni, M.1    Furumura, H.2    Kafuku, Y.3    Ishida, T.4    Inoue, M.5
  • 46
    • 0025992467 scopus 로고
    • Co-operative stacking and hydrogen bond pairing interactions of fragment peptides in cap binding protein with mRNA cap structure
    • Ueda, H., H. Igo, M Doi, M. Inoue and T. Ishida (1991) Co-operative stacking and hydrogen bond pairing interactions of fragment peptides in cap binding protein with mRNA cap structure Biochim. Biophys. Acta 1075, 181-186
    • (1991) Biochim. Biophys. Acta , vol.1075 , pp. 181-186
    • Ueda, H.1    Igo, H.2    Doi, M.3    Inoue, M.4    Ishida, T.5
  • 47
    • 0025394579 scopus 로고
    • The interaction of UVA radiation with cultured cells
    • Tyrrel, R. and S. Keyse (1990) The interaction of UVA radiation with cultured cells. J. Photochem. Photobiol. 4, 349-361
    • (1990) J. Photochem. Photobiol. , vol.4 , pp. 349-361
    • Tyrrel, R.1    Keyse, S.2
  • 48
    • 0017378282 scopus 로고
    • Studies on the interactions between DNA and flavins
    • Kuratomi, K. and Y. Kobayashi (1977) Studies on the interactions between DNA and flavins. Biochim. Biophys. Acta 476, 207-217.
    • (1977) Biochim. Biophys. Acta , vol.476 , pp. 207-217
    • Kuratomi, K.1    Kobayashi, Y.2
  • 49
    • 0020858268 scopus 로고
    • On the interaction between flavin-adenine rings and between flavin-indole rings by X-ray structural studies
    • Inoue, M., Y. Okuda, T. Ishida and M. Nakagaki (1983) On the interaction between flavin-adenine rings and between flavin-indole rings by X-ray structural studies. Arch. Biochem. Biophys. 227, 52-70.
    • (1983) Arch. Biochem. Biophys. , vol.227 , pp. 52-70
    • Inoue, M.1    Okuda, Y.2    Ishida, T.3    Nakagaki, M.4


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