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Volumn 67, Issue 3-4, 2003, Pages 479-486

Comparative investigations of the effects of X- and UV-irradiation on lysozyme in the absence or presence of additives

Author keywords

Additives; Lysozyme; Modeling; Radiation damage; Structure and function

Indexed keywords

ABSORPTION SPECTROSCOPY; ADDITIVES; AMINO ACIDS; FLUORESCENCE; IRRADIATION; RADIATION DAMAGE; ULTRAVIOLET RADIATION; X RAYS;

EID: 0038695940     PISSN: 0969806X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-806X(03)00089-6     Document Type: Conference Paper
Times cited : (27)

References (38)
  • 1
    • 0014638668 scopus 로고
    • On the mechanism of the radiation-induced inactivation of lysozyme in dilute aqueous solution
    • Adams G.E., Willson R.L., Aldrich J.E., Cundall R.B. On the mechanism of the radiation-induced inactivation of lysozyme in dilute aqueous solution. Int. J. Radiat. Biol. 16:1969;333-342.
    • (1969) Int. J. Radiat. Biol. , vol.16 , pp. 333-342
    • Adams, G.E.1    Willson, R.L.2    Aldrich, J.E.3    Cundall, R.B.4
  • 2
    • 0014623144 scopus 로고
    • The radiation-induced inactivation of lysozyme
    • Aldrich J.E., Cundall R.B. The radiation-induced inactivation of lysozyme. Int. J. Radiat. Biol. 16:1969;343-358.
    • (1969) Int. J. Radiat. Biol. , vol.16 , pp. 343-358
    • Aldrich, J.E.1    Cundall, R.B.2
  • 4
    • 0030971178 scopus 로고    scopus 로고
    • · radical transformation in hen egg-white lysozyme. Effects of pH, temperature, Trp62 oxidation and inhibitor binding
    • · radical transformation in hen egg-white lysozyme. Effects of pH, temperature, Trp62 oxidation and inhibitor binding. Biophys. Chem. 63:1997;153-166.
    • (1997) Biophys. Chem. , vol.63 , pp. 153-166
    • Bobrowski, K.1    Holcman, J.2    Poznanski, J.3    Wierzchowski, K.L.4
  • 5
    • 0024354001 scopus 로고
    • Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme
    • Brooks III C.L., Karplus M. Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme. J. Mol. Biol. 208:1989;159-181.
    • (1989) J. Mol. Biol. , vol.208 , pp. 159-181
    • Brooks C.L. III1    Karplus, M.2
  • 7
    • 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. 39:1984;537-562.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 537-562
    • Creed, D.1
  • 8
    • 84989674897 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids - II. Tyrosine and its simple derivatives
    • Creed D. The photophysics and photochemistry of the near-UV absorbing amino acids - II. Tyrosine and its simple derivatives. Photochem. Photobiol. 39:1984;563-575.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 563-575
    • Creed, D.1
  • 9
    • 84989726450 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids - III. Cystine and its simple derivatives
    • Creed D. The photophysics and photochemistry of the near-UV absorbing amino acids - III. Cystine and its simple derivatives. Photochem. Photobiol. 39:1984;577-583.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 577-583
    • Creed, D.1
  • 10
    • 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. 262:1987;9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 11
    • 0024384199 scopus 로고
    • Pulse radiolytic measurement of redox potentials. The tyrosine and tryptophan radicals
    • DeFilippis M.R., Murthy C.P., Faraggi M., Klapper M.H. Pulse radiolytic measurement of redox potentials. The tyrosine and tryptophan radicals. Biochemistry. 28:1989;4847-4853.
    • (1989) Biochemistry , vol.28 , pp. 4847-4853
    • DeFilippis, M.R.1    Murthy, C.P.2    Faraggi, M.3    Klapper, M.H.4
  • 12
    • 17044443531 scopus 로고    scopus 로고
    • Strategies for the spectroscopic characterization of irradiated proteins and other biomolecules
    • Durchschlag H. Strategies for the spectroscopic characterization of irradiated proteins and other biomolecules. J. Mol. Struct. 565-566:2001;197-203.
    • (2001) J. Mol. Struct. , vol.565-566 , pp. 197-203
    • Durchschlag, H.1
  • 16
    • 0038466911 scopus 로고
    • Transfert électronique intramoléculaire à longue distance dans les peptides et protéines
    • Faraggi M., Klapper M.H. Transfert électronique intramoléculaire à longue distance dans les peptides et protéines. J. Chim. Phys. 88:1991;1009-1019.
    • (1991) J. Chim. Phys. , vol.88 , pp. 1009-1019
    • Faraggi, M.1    Klapper, M.H.2
  • 17
    • 0030966337 scopus 로고    scopus 로고
    • Inactivation of hen egg-white lysozyme. The azide radical
    • Faraggi M., Bettelheim E., Weinstein M. Inactivation of hen egg-white lysozyme. The azide radical. J. Chim. Phys. 94:1997;356-364.
    • (1997) J. Chim. Phys. , vol.94 , pp. 356-364
    • Faraggi, M.1    Bettelheim, E.2    Weinstein, M.3
  • 18
    • 0027370327 scopus 로고
    • Oxidative damage to lysozyme by the hydroxyl radical: Comparative effects of scavengers
    • Franzini E., Sellak H., Hakim J., Pasquier C. Oxidative damage to lysozyme by the hydroxyl radical. comparative effects of scavengers Biochim. Biophys. Acta. 1203:1993;11-17.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 11-17
    • Franzini, E.1    Sellak, H.2    Hakim, J.3    Pasquier, C.4
  • 19
    • 0000798252 scopus 로고
    • Pulse radiolysis of aromatic amino acids - State of the art
    • Getoff N. Pulse radiolysis of aromatic amino acids - state of the art. Amino acids. 2:1992;195-214.
    • (1992) Amino acids , vol.2 , pp. 195-214
    • Getoff, N.1
  • 20
    • 0016927359 scopus 로고
    • Photochemical inactivation of enzymes
    • Grossweiner L.I. Photochemical inactivation of enzymes. Curr. Top. Radiat. Res. Q. 11:1976;141-199.
    • (1976) Curr. Top. Radiat. Res. Q. , vol.11 , pp. 141-199
    • Grossweiner, L.I.1
  • 22
    • 85047675865 scopus 로고
    • Dimer formation in radiation-irradiated aqueous solution of lysozyme studied by light-scattering-intensity measurement
    • Hashimoto S., Seki H., Masuda T., Imamura M., Kondo M. Dimer formation in radiation-irradiated aqueous solution of lysozyme studied by light-scattering-intensity measurement. Int. J. Radiat. Biol. 40:1981;31-46.
    • (1981) Int. J. Radiat. Biol. , vol.40 , pp. 31-46
    • Hashimoto, S.1    Seki, H.2    Masuda, T.3    Imamura, M.4    Kondo, M.5
  • 23
    • 0021701864 scopus 로고
    • The repair of oxidized amino acids by antioxidants
    • Hoey B.M., Butler J. The repair of oxidized amino acids by antioxidants. Biochim. Biophys. Acta. 791:1984;212-218.
    • (1984) Biochim. Biophys. Acta , vol.791 , pp. 212-218
    • Hoey, B.M.1    Butler, J.2
  • 24
    • 0018538777 scopus 로고
    • Applications of pulse radiolysis to protein chemistry
    • Klapper M.H., Faraggi M. Applications of pulse radiolysis to protein chemistry. Q. Rev. Biophys. 12:1979;465-519.
    • (1979) Q. Rev. Biophys. , vol.12 , pp. 465-519
    • Klapper, M.H.1    Faraggi, M.2
  • 25
    • 0000800911 scopus 로고
    • Hydration of macromolecules. III. Hydration of polypeptides
    • Kuntz I.D. Hydration of macromolecules. III. Hydration of polypeptides. J. Am. Chem. Soc. 93:1971;514-516.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 514-516
    • Kuntz, I.D.1
  • 26
    • 0016220239 scopus 로고
    • Structural damage in γ-irradiated lysozyme
    • Marciani D.J., Tolbert B.M. Structural damage in γ-irradiated lysozyme. Biochim. Biophys. Acta. 351:1974;387-395.
    • (1974) Biochim. Biophys. Acta , vol.351 , pp. 387-395
    • Marciani, D.J.1    Tolbert, B.M.2
  • 30
    • 34247124903 scopus 로고
    • The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme
    • Shugar D. The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme. Biochim. Biophys. Acta. 8:1952;302-309.
    • (1952) Biochim. Biophys. Acta , vol.8 , pp. 302-309
    • Shugar, D.1
  • 31
    • 0021179020 scopus 로고
    • Resolved multisite OH-attack on aqueous tryptophan studied by pulse radiolysis
    • Solar S., Solar W., Getoff N. Resolved multisite OH-attack on aqueous tryptophan studied by pulse radiolysis. Radiat. Phys. Chem. 23:1984;371-376.
    • (1984) Radiat. Phys. Chem. , vol.23 , pp. 371-376
    • Solar, S.1    Solar, W.2    Getoff, N.3
  • 32
    • 0000612902 scopus 로고
    • Reactivity of OH with tyrosine in aqueous solution studied by pulse radiolysis
    • Solar S., Solar W., Getoff N. Reactivity of OH with tyrosine in aqueous solution studied by pulse radiolysis. J. Phys. Chem. 88:1984;2091-2095.
    • (1984) J. Phys. Chem. , vol.88 , pp. 2091-2095
    • Solar, S.1    Solar, W.2    Getoff, N.3
  • 34
    • 0024725276 scopus 로고
    • Role of thiols in radioprotection: Radiation chemical aspects
    • Tamba M. Role of thiols in radioprotection. radiation chemical aspects Z. Naturforsch. 44c:1989;857-862.
    • (1989) Z. Naturforsch. , vol.44 C , pp. 857-862
    • Tamba, M.1
  • 35
    • 0023809513 scopus 로고
    • Photooxidative changes of lysozyme with 337.1 nm laser radiation
    • VanderMeulen D.L., Judy M.M. Photooxidative changes of lysozyme with 337.1. nm laser radiation Radiat. Environ. Biophys. 27:1988;307-316.
    • (1988) Radiat. Environ. Biophys. , vol.27 , pp. 307-316
    • VanderMeulen, D.L.1    Judy, M.M.2
  • 36
    • 0014771842 scopus 로고
    • Photochemical reactions in amino acid residues and inactivation of enzymes during UV-irradiation. A review
    • Vladimirov Yu.A., Roshchupkin D.I., Fesenko E.E. Photochemical reactions in amino acid residues and inactivation of enzymes during UV-irradiation. A review. Photochem. Photobiol. 11:1970;227-246.
    • (1970) Photochem. Photobiol. , vol.11 , pp. 227-246
    • Vladimirov, Yu.A.1    Roshchupkin, D.I.2    Fesenko, E.E.3
  • 37
    • 0030793507 scopus 로고    scopus 로고
    • SIMS: Computation of a smooth invariant molecular surface
    • Vorobjev Y.N., Hermans J. SIMS. computation of a smooth invariant molecular surface Biophys. J., 73:1997;722-732.
    • (1997) Biophys. J., , vol.73 , pp. 722-732
    • Vorobjev, Y.N.1    Hermans, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.