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Volumn 56, Issue 12, 2008, Pages 4720-4725

Tryptophan-mediated denaturation of β-lactoglobulin A by UV irradiation

Author keywords

lactoglobulin; Disulfide; Photo oxidation; Tryptophan; UV irradiation

Indexed keywords

LACTOGLOBULIN; THIOL DERIVATIVE; TRYPTOPHAN;

EID: 47349111403     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0733158     Document Type: Article
Times cited : (44)

References (27)
  • 2
    • 84980156189 scopus 로고
    • The photolysis of free cystine in the presence of aromatic amino acids
    • Dose, K. The photolysis of free cystine in the presence of aromatic amino acids. Photochem. Photobiol. 1968, 8, 331-335.
    • (1968) Photochem. Photobiol , vol.8 , pp. 331-335
    • Dose, K.1
  • 3
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y.; Barkley, M. D. Toward understanding tryptophan fluorescence in proteins. Biochemistry 1998, 37, 9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 4
    • 0032817737 scopus 로고    scopus 로고
    • Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase
    • Prompers, J. J.; Hilbers, C. W.; Pepermans, H. A. M. Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase. FEBS Lett. 1999, 456, 409-416.
    • (1999) FEBS Lett , vol.456 , pp. 409-416
    • Prompers, J.J.1    Hilbers, C.W.2    Pepermans, H.A.M.3
  • 7
    • 0036712109 scopus 로고    scopus 로고
    • Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin
    • Vanhooren, A.; Devreese, B.; Vanhee, K.; Van Beeumen, J.; Hanssens, I. Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin. Biochemistry 2002, 41, 11035-11043.
    • (2002) Biochemistry , vol.41 , pp. 11035-11043
    • Vanhooren, A.1    Devreese, B.2    Vanhee, K.3    Van Beeumen, J.4    Hanssens, I.5
  • 8
    • 0042236699 scopus 로고    scopus 로고
    • Fourier transform IR attenuated total reflectance spectroscopy studies of cysteine-induced changes in secondary conformations of bovine serum albumin after UV-B irradiation
    • Wei, Y.-S.; Lin, S.-Y.; Wang, S.-L.; Li, M.-J.; Cheng, W.-T. Fourier transform IR attenuated total reflectance spectroscopy studies of cysteine-induced changes in secondary conformations of bovine serum albumin after UV-B irradiation. Biopolymers 2003, 72, 345-351.
    • (2003) Biopolymers , vol.72 , pp. 345-351
    • Wei, Y.-S.1    Lin, S.-Y.2    Wang, S.-L.3    Li, M.-J.4    Cheng, W.-T.5
  • 9
  • 10
    • 1542575976 scopus 로고    scopus 로고
    • Heat-induced denaturation/ aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed
    • Croguennec, T.; O'Kennedy, B. T.; Mehra, R. Heat-induced denaturation/ aggregation of β-lactoglobulin A and B: kinetics of the first intermediates formed. Int. Dairy J. 2004, 14, 399-409.
    • (2004) Int. Dairy J , vol.14 , pp. 399-409
    • Croguennec, T.1    O'Kennedy, B.T.2    Mehra, R.3
  • 11
    • 3042934967 scopus 로고
    • Tissue sulphydryl groups
    • Ellman, G. L. Tissue sulphydryl groups. Arch. Biochem. Biophys. 1959, 82, 70-72.
    • (1959) Arch. Biochem. Biophys , vol.82 , pp. 70-72
    • Ellman, G.L.1
  • 12
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid) - a reexamination
    • Riddles, P. W.; Blakeley, R. L.; Zerner, B. Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid) - a reexamination. Anal. Biochem. 1979, 94, 75-81.
    • (1979) Anal. Biochem , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 14
    • 0037423721 scopus 로고    scopus 로고
    • Stable monomelic intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin
    • Croguennec, T.; Bouhallab, S.; Mollé, D.; O'Kennedy, B. T.; Mehra, R. Stable monomelic intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin. Biochem. Biophys. Res. Commun. 2003, 301, 465-471.
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , pp. 465-471
    • Croguennec, T.1    Bouhallab, S.2    Mollé, D.3    O'Kennedy, B.T.4    Mehra, R.5
  • 15
    • 0027323183 scopus 로고
    • Secondary structure and temperature-induced unfolding and refolding of ribonuclease-T(1) in aqueous-solution - a Fourier-transform infrared spectroscopic study
    • Fabian, H.; Schultz, C.; Naumann, D.; Landt, O.; Hahn, U.; Saenger, W. Secondary structure and temperature-induced unfolding and refolding of ribonuclease-T(1) in aqueous-solution - a Fourier-transform infrared spectroscopic study. J. Mol. Biol. 1993, 232, 967-981.
    • (1993) J. Mol. Biol , vol.232 , pp. 967-981
    • Fabian, H.1    Schultz, C.2    Naumann, D.3    Landt, O.4    Hahn, U.5    Saenger, W.6
  • 16
    • 0026516588 scopus 로고
    • Halogenated alcohols as solvents for proteins - FTIR spectroscopic studies
    • Jackson, M.; Mantsch, H. H. Halogenated alcohols as solvents for proteins - FTIR spectroscopic studies. Biochim. Biophys. Acta 1992, 1118, 139-143.
    • (1992) Biochim. Biophys. Acta , vol.1118 , pp. 139-143
    • Jackson, M.1    Mantsch, H.H.2
  • 17
    • 0019536747 scopus 로고
    • Infrared and laser-raman spectroscopic studies of thermally-induced globular protein gels
    • Clark, A. H.; Saunderson, D. H. P.; Suggett, A. Infrared and laser-raman spectroscopic studies of thermally-induced globular protein gels. Int. J. Pept. Protein Res. 1981, 17, 353-364.
    • (1981) Int. J. Pept. Protein Res , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.P.2    Suggett, A.3
  • 18
    • 0034578634 scopus 로고    scopus 로고
    • Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels
    • Lefèvre, T.; Subirade, M. Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels. Biopolymers 2000, 54, 578-586.
    • (2000) Biopolymers , vol.54 , pp. 578-586
    • Lefèvre, T.1    Subirade, M.2
  • 19
    • 0642302370 scopus 로고    scopus 로고
    • Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins A and B
    • Boye, J. I.; Ma, C. Y.; Ismail, A.; Harwalkar, V. R.; Kalab, M. Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins A and B. J. Agric. Food Chem. 1997, 45, 1608-1618.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 1608-1618
    • Boye, J.I.1    Ma, C.Y.2    Ismail, A.3    Harwalkar, V.R.4    Kalab, M.5
  • 20
    • 0023693897 scopus 로고
    • Structural and conformational-changes of β-lactoglobulin B - an infrared spectroscopic study of the effect of pH and temperature
    • Casal, H. L.; Kohler, U.; Mantsch, H. H. Structural and conformational-changes of β-lactoglobulin B - an infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta 1988, 957, 11-20.
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 11-20
    • Casal, H.L.1    Kohler, U.2    Mantsch, H.H.3
  • 21
    • 84989712905 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids - I. Tryptophan and its simple derivatives
    • Creed, D. The photophysics and photochemistry of the near-UV absorbing amino acids - I. Tryptophan and its simple derivatives. Photochem. Photobiol. 1984, 39, 537-562.
    • (1984) Photochem. Photobiol , vol.39 , pp. 537-562
    • Creed, D.1
  • 22
    • 0021344070 scopus 로고
    • Photochemistry of proteins: A review
    • Grossweiner, L. I. Photochemistry of proteins: a review. Curr. Eye Res. 1984, 3, 137-144.
    • (1984) Curr. Eye Res , vol.3 , pp. 137-144
    • Grossweiner, L.I.1
  • 23
    • 0042581103 scopus 로고
    • Electronic properties of N-formylkynurenine and related compounds
    • Pileni, M.-P.; Walrant, P.; Santus, R. Electronic properties of N-formylkynurenine and related compounds. J. Phys. Chem. 1976, 80, 1804-1809.
    • (1976) J. Phys. Chem , vol.80 , pp. 1804-1809
    • Pileni, M.-P.1    Walrant, P.2    Santus, R.3
  • 24
    • 0028567981 scopus 로고
    • A model of the denaturation and aggregation of β-lactoglobulin
    • Roefs, S. P. F. M.; de Kruif, K. G. A model of the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem. 1994, 226, 883-889.
    • (1994) Eur. J. Biochem , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    de Kruif, K.G.2
  • 25
    • 1942441014 scopus 로고    scopus 로고
    • Spectroscopic characterisation of heat-induced nonnative β-lactoglobulin monomers
    • Croguennec, T.; Molle, D.; Mehra, R.; Bouhallab, S. Spectroscopic characterisation of heat-induced nonnative β-lactoglobulin monomers. Protein Sci. 2004, 13, 1340-1346.
    • (2004) Protein Sci , vol.13 , pp. 1340-1346
    • Croguennec, T.1    Molle, D.2    Mehra, R.3    Bouhallab, S.4
  • 26
    • 0032839589 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence
    • Manderson, G. A.; Hardman, M. J.; Creamer, L. K. Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence. J. Agric. Food Chem. 1999, 47, 3617-3627.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 3617-3627
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 27
    • 0030078033 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin
    • Stapelfeldt, H.; Petersen, P. H.; Kristiansen, K. R.; Qvist, K. B.; Skibsted, L. H. Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin. J. Dairy Res. 1996, 63, 111-118.
    • (1996) J. Dairy Res , vol.63 , pp. 111-118
    • Stapelfeldt, H.1    Petersen, P.H.2    Kristiansen, K.R.3    Qvist, K.B.4    Skibsted, L.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.