메뉴 건너뛰기




Volumn 45, Issue 7, 2006, Pages 2085-2093

Selectivity of tryptophan residues in mediating photolysis of disulfide bridges in goat α-lactalbumin

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CHEMICAL REACTIONS; MASS SPECTROMETRY; POLYPEPTIDES; PROTEINS;

EID: 33144461891     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0517638     Document Type: Article
Times cited : (24)

References (26)
  • 1
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins, C. L., and Davies, M. J. (2001) Generation and propagation of radical reactions on proteins, Biochim. Biophys. Acta 1504, 196-219.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 2
    • 0037564169 scopus 로고    scopus 로고
    • Singlet oxygen-mediated damage to proteins and its consequences
    • Davies, M. J. (2003) Singlet oxygen-mediated damage to proteins and its consequences, Biochem. Biophys. Res. Commun. 305, 761-770.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 761-770
    • Davies, M.J.1
  • 3
    • 0035473032 scopus 로고    scopus 로고
    • Photo-oxidation of proteins and its role in cataractogenesis
    • Davies, M. J., and Truscott, R. J. W. (2001) Photo-oxidation of proteins and its role in cataractogenesis, J. Photochem. Photobiol., B 63, 114-125.
    • (2001) J. Photochem. Photobiol., B , vol.63 , pp. 114-125
    • Davies, M.J.1    Truscott, R.J.W.2
  • 4
    • 84989712905 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids. 1. Tryptophan and its simple derivatives
    • Creed, D. (1984) The photophysics and photochemistry of the near-UV absorbing amino acids. 1. Tryptophan and its simple derivatives, Photochem. Photobiol. 39, 537-562.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 537-562
    • Creed, D.1
  • 5
    • 84980156189 scopus 로고
    • The phololysis of free cystine in the presence of aromatic amino acids
    • Dose, K. (1968) The phololysis of free cystine in the presence of aromatic amino acids, Photochem. Photobiol. 8, 331-335.
    • (1968) Photochem. Photobiol. , vol.8 , pp. 331-335
    • Dose, K.1
  • 6
    • 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., and Pepermans, H. A. M. (1999) Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase, FEBS Letters 456, 409-416.
    • (1999) FEBS Letters , vol.456 , pp. 409-416
    • Prompers, J.J.1    Hilbers, C.W.2    Pepermans, H.A.M.3
  • 7
    • 0036712109 scopus 로고    scopus 로고
    • Tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin
    • Vanhooren, A., Devreese, B., Vanhee, K., Van Beeumen, J., and Hanssens, I. (2002) Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin, Biochemistry 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
  • 9
    • 0041709212 scopus 로고    scopus 로고
    • Solid-state photodegradation of bovine somatotropin (bovine growth hormone): Evidence for tryptophan-mediated photooxidation of disulfide bonds
    • Miller, B. L., Hageman, M. J., Thamann, T. J., Barron, L. B., and Schoneich, C. (2003) Solid-state photodegradation of bovine somatotropin (bovine growth hormone): Evidence for tryptophan-mediated photooxidation of disulfide bonds, J. Pharm. Sci. 92, 1698-1709.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 1698-1709
    • Miller, B.L.1    Hageman, M.J.2    Thamann, T.J.3    Barron, L.B.4    Schoneich, C.5
  • 10
    • 19544362355 scopus 로고    scopus 로고
    • Tryptophan to phenylalanine substitution allows to differentiate between short and long range conformational changes during denaturation of goat α-lactalbumin
    • Vanhooren, A., Chedad, A., Farkas, V., Majer, Z., Van Dael, H., Joniau, M., and Hanssens, I. (2005) Tryptophan to phenylalanine substitution allows to differentiate between short and long range conformational changes during denaturation of goat α-lactalbumin, Proteins 60, 118-130.
    • (2005) Proteins , vol.60 , pp. 118-130
    • Vanhooren, A.1    Chedad, A.2    Farkas, V.3    Majer, Z.4    Van Dael, H.5    Joniau, M.6    Hanssens, I.7
  • 12
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 13
    • 0014251737 scopus 로고
    • The role of α-lactalbumin and the a protein in lactose synthetase: A unique mechanism for the control of a biological reaction
    • Brew, K., Vanaman, T. C., Hill, R. L. (1968) The role of α-lactalbumin and the A protein in lactose synthetase: A unique mechanism for the control of a biological reaction, Proc. Natl. Acad. Sci. U.S.A. 59, 491-497.
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.59 , pp. 491-497
    • Brew, K.1    Vanaman, T.C.2    Hill, R.L.3
  • 14
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups, Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 15
    • 0032859790 scopus 로고    scopus 로고
    • 5,5′-dithiobis-(2-nitrobenzoic acid) as a probe for a non-essential cysteine residue at the medium chain acyl-coenzyme? A dehydrogenase binding site of the human 'electron transferring flavoprotein' (ETF)
    • Parker, A., and Engel, P. C. (1999) 5,5′-Dithiobis-(2-nitrobenzoic acid) as a probe for a non-essential cysteine residue at the medium chain acyl-coenzyme? A dehydrogenase binding site of the human 'electron transferring flavoprotein' (ETF), J. Enzymol. Inhib. Med. Chem. 14, 381-390.
    • (1999) J. Enzymol. Inhib. Med. Chem. , vol.14 , pp. 381-390
    • Parker, A.1    Engel, P.C.2
  • 16
    • 0019000261 scopus 로고
    • Intermolecular and intramolecular interactions of α-lactalbumin: Comparative fluorescence properties of bovine, goat, human and guinea-pig α-lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers
    • Sommers, P. B., and Kronman, M. J. (1980) Intermolecular and intramolecular interactions of α-lactalbumin: Comparative fluorescence properties of bovine, goat, human and guinea-pig α-lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers, Biophys. Chem. 11, 217-232.
    • (1980) Biophys. Chem. , vol.11 , pp. 217-232
    • Sommers, P.B.1    Kronman, M.J.2
  • 18
    • 4544250589 scopus 로고    scopus 로고
    • Kinetics of folding and unfolding of goat α-lactalbumin
    • Chedad, A., and Van Dael, H. (2004) Kinetics of folding and unfolding of goat α-lactalbumin, Proteins 57, 345-356.
    • (2004) Proteins , vol.57 , pp. 345-356
    • Chedad, A.1    Van Dael, H.2
  • 19
    • 28044462676 scopus 로고    scopus 로고
    • Influence of Trp mutation on native, intermediate, and transition states of goat α-lactalbumin: An equilibrium and kinetic study
    • Chedad, A., Van Dael, H., Vanhooren A., and Hanssens, I. (2005) Influence of Trp mutation on native, intermediate, and transition states of goat α-lactalbumin: An equilibrium and kinetic study, Biochemistry 44, 15129-15138.
    • (2005) Biochemistry , vol.44 , pp. 15129-15138
    • Chedad, A.1    Van Dael, H.2    Vanhooren, A.3    Hanssens, I.4
  • 20
    • 0028095491 scopus 로고
    • Study by mutagenesis of the roles of 2 aromatic clusters of α-lactalbumin in aspects of its action in the lactose synthase system
    • Grobler, J. A., Wang, M., Pike, A. C. W., and Brew, K. (1994) Study by mutagenesis of the roles of 2 aromatic clusters of α-lactalbumin in aspects of its action in the lactose synthase system, J. Biol. Chem. 269, 5106-5114.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5106-5114
    • Grobler, J.A.1    Wang, M.2    Pike, A.C.W.3    Brew, K.4
  • 22
    • 0028916267 scopus 로고
    • Local structural preferences in the α-lactalbumin molten globule
    • Peng, Z. Y., Wu, L. C., and Kim, P. S. (1995) Local structural preferences in the α-lactalbumin molten globule, Biochemistry 34, 3248-3252.
    • (1995) Biochemistry , vol.34 , pp. 3248-3252
    • Peng, Z.Y.1    Wu, L.C.2    Kim, P.S.3
  • 23
    • 0030585408 scopus 로고    scopus 로고
    • Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase
    • Pike, A. C. W., Brew, K., and Acharya, K. R. (1996) Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase, Structure 4, 691-703.
    • (1996) Structure , vol.4 , pp. 691-703
    • Pike, A.C.W.1    Brew, K.2    Acharya, K.R.3
  • 24
    • 0346613555 scopus 로고    scopus 로고
    • Reaction of HOCl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation, reactions of nitrogen-centred radicals
    • Hawkins, C. L., and Davies, M. J. (1998) Reaction of HOCl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation, reactions of nitrogen-centred radicals, J. Chem. Soc., Perkin Trans. 2, 1937-1945.
    • (1998) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1937-1945
    • Hawkins, C.L.1    Davies, M.J.2
  • 25
    • 0037192149 scopus 로고    scopus 로고
    • Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: A potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase
    • Fu, X. Y., Mueller, D. M., and Heinecke, J. W. (2002) Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: A potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase, Biochemistry 41, 1293-1301.
    • (2002) Biochemistry , vol.41 , pp. 1293-1301
    • Fu, X.Y.1    Mueller, D.M.2    Heinecke, J.W.3
  • 26
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-model and the Swiss-PDB viewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) Swiss-model and the Swiss-PDB viewer: An environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.