메뉴 건너뛰기




Volumn 76, Issue 5, 2000, Pages 673-681

Protein γ-radiolysis in frozen solutions is a macromolecular surface phenomenon: Fragmentation of lysozyme, citrate synthase and α-lactalbumin in native or denatured states

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LACTALBUMIN; CITRATE SYNTHASE; COBALT 60; LYSOZYME; UREA;

EID: 0034120377     PISSN: 09553002     EISSN: None     Source Type: Journal    
DOI: 10.1080/095530000138349     Document Type: Article
Times cited : (12)

References (52)
  • 2
    • 0013675805 scopus 로고
    • The relative roles of ionization and excitation processes in radiation inactivation of enzymes
    • AUGENSTEIN, L. G., BRUSTAD, T. and MASON, R., 1964, The relative roles of ionization and excitation processes in radiation inactivation of enzymes. Advances in Radiation Biology, 1, 227-266.
    • (1964) Advances in Radiation Biology , vol.1 , pp. 227-266
    • Augenstein, L.G.1    Brustad, T.2    Mason, R.3
  • 3
    • 0023072444 scopus 로고
    • The radiation inactivation method as a tool to study structure-function relationships in proteins
    • BEAUREGARD, G., MARET, A., SALVAYRE, R. and POTIER, M., 1987, The radiation inactivation method as a tool to study structure-function relationships in proteins. Methods in Biochemical Analysis, 32, 313-343.
    • (1987) Methods in Biochemical Analysis , vol.32 , pp. 313-343
    • Beauregard, G.1    Maret, A.2    Salvayre, R.3    Potier, M.4
  • 5
    • 0013671702 scopus 로고    scopus 로고
    • Response to the comments of Dr Kempner
    • BEROVIC, N., 1996, Response to the comments of Dr Kempner. Radiation Research, 145, 650-651.
    • (1996) Radiation Research , vol.145 , pp. 650-651
    • Berovic, N.1
  • 7
    • 0026681622 scopus 로고
    • mRNP4, a major mRNA-binding protein from Xenopus oocytes is identical to transcription factor FRGY2
    • DESCHAMPS, S., VIEL, A., GARRIGOS, M., DENIS, H. and LE MAIRE, M., 1992, mRNP4, a major mRNA-binding protein from Xenopus oocytes is identical to transcription factor FRGY2. Journal of Biological Chemistry, 267, 13799-13802.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 13799-13802
    • Deschamps, S.1    Viel, A.2    Garrigos, M.3    Denis, H.4    Le Maire, M.5
  • 8
    • 0015994218 scopus 로고
    • Real-space refinement of the structure of hen-egg-white lysozyme
    • DIAMOND, R., 1974, Real-space refinement of the structure of hen-egg-white lysozyme. Journal of Molecular Biology, 82, 371-391.
    • (1974) Journal of Molecular Biology , vol.82 , pp. 371-391
    • Diamond, R.1
  • 11
    • 0001529088 scopus 로고
    • Quasielastic light scattering from human alpha-lactalbumin: Comparison of molecular dimensions in native and 'molten globule' states
    • GAST, K., ZIRWER, D., WELFLE, H., BYCHKOVA, V. E. and PTITSYN, O. B., 1986, Quasielastic light scattering from human alpha-lactalbumin: comparison of molecular dimensions in native and 'molten globule' states. International Journal of Biological Macromolecules, 8, 231-236.
    • (1986) International Journal of Biological Macromolecules , vol.8 , pp. 231-236
    • Gast, K.1    Zirwer, D.2    Welfle, H.3    Bychkova, V.E.4    Ptitsyn, O.B.5
  • 12
    • 0030886655 scopus 로고    scopus 로고
    • Fe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: Evidence for conformation-sensitive interactions between cytoplasmic domains
    • GOLDSHLEGER, R. and KARLISH, S. J. D., 1997, Fe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domains. Proceedings of the National Academy of Sciences of the United States of America, 94, 9596-9601.
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , pp. 9596-9601
    • Goldshleger, R.1    Karlish, S.J.D.2
  • 15
    • 0030139066 scopus 로고
    • Comments on 'A critical analysis of the use of radiation inactivation to measure the mass of protein' by Lidzey et al
    • Radiat Res 143, 181-186, 1995
    • KEMPNER, E. S., 1990, Comments on 'A critical analysis of the use of radiation inactivation to measure the mass of protein' by Lidzey et al. (Radiat Res 143, 181-186, 1995). Radiation Research, 145, 649-650.
    • (1990) Radiation Research , vol.145 , pp. 649-650
    • Kempner, E.S.1
  • 16
    • 0018400554 scopus 로고
    • Size determination of enzymes by radiation inactivation
    • KEMPNER, E. S. and SCHLEGEL, W., 1979, Size determination of enzymes by radiation inactivation. Analytical Biochemistry, 92, 2-10.
    • (1979) Analytical Biochemistry , vol.92 , pp. 2-10
    • Kempner, E.S.1    Schlegel, W.2
  • 17
    • 0014421587 scopus 로고
    • Membrane enzyme systems. Molecular size determinations by radiation inactivation
    • KEPNER, G. R. and MACEY, R. I., 1968, Membrane enzyme systems. Molecular size determinations by radiation inactivation. Biochimica Biophysica Acta, 163, 188-203.
    • (1968) Biochimica Biophysica Acta , vol.163 , pp. 188-203
    • Kepner, G.R.1    Macey, R.I.2
  • 18
    • 0029165821 scopus 로고
    • Photodynamic and radiolytic inactivation of ion channels formed by gramicidin A: Oxidation and fragmentation
    • KUNZ, L., ZEIDLER, U., HAEGELE, K., PRZYBYLSKI, M. and STARK, G., 1995, Photodynamic and radiolytic inactivation of ion channels formed by gramicidin A: oxidation and fragmentation. Biochemistry, 34, 11895-11903.
    • (1995) Biochemistry , vol.34 , pp. 11895-11903
    • Kunz, L.1    Zeidler, U.2    Haegele, K.3    Przybylski, M.4    Stark, G.5
  • 19
    • 0024417964 scopus 로고
    • The molten globular state as a due for understanding the folding and cooperativity of globular-protein structure
    • KUWAJIMA, K., 1989, The molten globular state as a due for understanding the folding and cooperativity of globular-protein structure. Proteins: Structure Function and Genetics, 6, 87-103.
    • (1989) Proteins: Structure Function and Genetics , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 20
    • 0026767871 scopus 로고
    • Long range electron transfer along an alpha-helix
    • LEE, H., FARAGGI, M. and KLAPPER, M. H., 1992, Long range electron transfer along an alpha-helix. Biochimica Biophysica Acta, 1159, 286-294.
    • (1992) Biochimica Biophysica Acta , vol.1159 , pp. 286-294
    • Lee, H.1    Faraggi, M.2    Klapper, M.H.3
  • 21
    • 0022453762 scopus 로고
    • The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: A caution and a list of membrane proteins suitable as standards
    • LE MAIRE, M., AGGERBECK, L. P., MONTEILHET, C., ANDERSEN, J. P. and MØLLER, J. V., 1986, The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: a caution and a list of membrane proteins suitable as standards. Analytical Biochemistry, 154, 525-535.
    • (1986) Analytical Biochemistry , vol.154 , pp. 525-535
    • Le Maire, M.1    Aggerbeck, L.P.2    Monteilhet, C.3    Andersen, J.P.4    Møller, J.V.5
  • 22
    • 0020696009 scopus 로고
    • Size and shape of detergent-solubilized photochemical reaction centers form two strains of Rhodopseudomononas spheroide: A solution X-ray scattering study
    • LE MAIRE, M. and RIVAS, E., 1983, Size and shape of detergent-solubilized photochemical reaction centers form two strains of Rhodopseudomononas spheroide: a solution X-ray scattering study. Biochimica Biophysica Acta, 722, 150-157.
    • (1983) Biochimica Biophysica Acta , vol.722 , pp. 150-157
    • Le Maire, M.1    Rivas, E.2
  • 23
    • 0025248416 scopus 로고
    • Effects of ionizing radiation on proteins. Evidence of non-random fragmentations and a caution in the use of the method for determination of molecular mass
    • LE MAIRE, M., THAUVETTE, L., DE FORESTA, B., VIEL, A., BEAUREGARD, G. and POTIER, M., 1990, Effects of ionizing radiation on proteins. Evidence of non-random fragmentations and a caution in the use of the method for determination of molecular mass. Biochemical Journal, 267, 431-439.
    • (1990) Biochemical Journal , vol.267 , pp. 431-439
    • Le Maire, M.1    Thauvette, L.2    De Foresta, B.3    Viel, A.4    Beauregard, G.5    Potier, M.6
  • 25
    • 0030896850 scopus 로고    scopus 로고
    • Effects of free radicals on partial reactions of the Na.K-ATPase
    • MENSE, M., STARK, G. and APELL, H.J., 1997, Effects of free radicals on partial reactions of the Na.K-ATPase. Journal of Membrane Biology, 156, 63-71.
    • (1997) Journal of Membrane Biology , vol.156 , pp. 63-71
    • Mense, M.1    Stark, G.2    Apell, H.J.3
  • 26
    • 0029074884 scopus 로고
    • Time-course studies by neutron solution scattering and biochemical assays of the aggregation of human low-density lipoprotein during Cu(2 + )-induced oxidation
    • MFYER, D. F., MAYANS, M. O., GROOT, P. H., SUCKLING, K. E., BRUCKDORFER, K. R. and PERKINS, S. J.. 1995, Time-course studies by neutron solution scattering and biochemical assays of the aggregation of human low-density lipoprotein during Cu(2 + )-induced oxidation. Biochemical Journal, 310, 417-426.
    • (1995) Biochemical Journal , vol.310 , pp. 417-426
    • Mfyer, D.F.1    Mayans, M.O.2    Groot, P.H.3    Suckling, K.E.4    Bruckdorfer, K.R.5    Perkins, S.J.6
  • 27
    • 0023050401 scopus 로고
    • Molecular-size standards for use in radiation-inactivation studies on proteins
    • NUGENT, J. H. A., 1986. Molecular-size standards for use in radiation-inactivation studies on proteins. Biochemical Journal, 239, 459-462.
    • (1986) Biochemical Journal , vol.239 , pp. 459-462
    • Nugent, J.H.A.1
  • 28
    • 0030883587 scopus 로고    scopus 로고
    • Endogenous basic fibroblast growth factor isoforms involved in different intracellular protein complexes
    • PATRY, V., BUGLER, B., MARET, A., POTIER, M. and PRATS, H., 1997, Endogenous basic fibroblast growth factor isoforms involved in different intracellular protein complexes. Biochemical Journal, 326, 259-264.
    • (1997) Biochemical Journal , vol.326 , pp. 259-264
    • Patry, V.1    Bugler, B.2    Maret, A.3    Potier, M.4    Prats, H.5
  • 30
    • 0026040834 scopus 로고
    • Inactivation mechanism of tetrameric β-galactosidase by γ-rays involves both fragmentation and temperature-dependent denaturation of proteins
    • POTIER, M., THAUVETTE, L., MICHAUD, L., GIROUX, S. and BEAUREGARD, G., 1991, Inactivation mechanism of tetrameric β-galactosidase by γ-rays involves both fragmentation and temperature-dependent denaturation of proteins. Biochemistry, 30, 8151-8157.
    • (1991) Biochemistry , vol.30 , pp. 8151-8157
    • Potier, M.1    Thauvette, L.2    Michaud, L.3    Giroux, S.4    Beauregard, G.5
  • 31
    • 0028269389 scopus 로고
    • Radiation inactivation of proteins: Temperature-dependent inter-protomeric energy transfer in ox liver catalase
    • POTIER, M., VILLEMFURE, J. F. and THAUVETTE, L., 1994, Radiation inactivation of proteins: temperature-dependent inter-protomeric energy transfer in ox liver catalase. Biochemical Journal, 298, 571-574.
    • (1994) Biochemical Journal , vol.298 , pp. 571-574
    • Potier, M.1    Villemfure, J.F.2    Thauvette, L.3
  • 32
    • 0028031337 scopus 로고
    • Direct observation of enzyme activity with the atomic force microscope
    • RADMACHER, M., FRITZ, M., HANSMA, H. G. and HANSMA, P. K., 1991, Direct observation of enzyme activity with the atomic force microscope. Science, 265, 1577-1579.
    • (1991) Science , vol.265 , pp. 1577-1579
    • Radmacher, M.1    Fritz, M.2    Hansma, H.G.3    Hansma, P.K.4
  • 33
    • 0020483375 scopus 로고
    • Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution
    • REMINGTON, S., WIEGAND, G. and HUKFR, R., 1982, Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. Journal of Molecular Biology, 158, 111-152.
    • (1982) Journal of Molecular Biology , vol.158 , pp. 111-152
    • Remington, S.1    Wiegand, G.2    Hukfr, R.3
  • 34
    • 0014940381 scopus 로고
    • The gross conformation of protein-sodium dodecyl sulfate complexes
    • REYNOLDS, J. A. and TANFORD, C., 1970a, The gross conformation of protein-sodium dodecyl sulfate complexes. Journal of Biological Chemistry, 245, 5161-5165.
    • (1970) Journal of Biological Chemistry , vol.245 , pp. 5161-5165
    • Reynolds, J.A.1    Tanford, C.2
  • 35
    • 0014816360 scopus 로고
    • Binding of dodecyl sulfate to protein at high binding ratios. Possible implications for the state of proteins in biological membranes
    • REYNOLDS, J. A. and TANFORD, C., 1970b, Binding of dodecyl sulfate to protein at high binding ratios. Possible implications for the state of proteins in biological membranes. Proceedings of the National Academy of Sciences of the United States of America, 66, 1002-1007.
    • (1970) Proceedings of the National Academy of Sciences of the United States of America , vol.66 , pp. 1002-1007
    • Reynolds, J.A.1    Tanford, C.2
  • 36
    • 0017179208 scopus 로고
    • Molecular weights and hydrophobicity of the polypeptide chain of sarcoplasmic reticulum calcium (II) adenosine triphosphatase and of its primary tryptic fragments
    • RIZZOLO, L. J., LE MAIRE, M., REYNOLDS, J. A. and TANFORD, C., 1976, Molecular weights and hydrophobicity of the polypeptide chain of sarcoplasmic reticulum calcium (II) adenosine triphosphatase and of its primary tryptic fragments. Biochemistry, 15, 3433-3437.
    • (1976) Biochemistry , vol.15 , pp. 3433-3437
    • Rizzolo, L.J.1    Le Maire, M.2    Reynolds, J.A.3    Tanford, C.4
  • 37
    • 0032190777 scopus 로고    scopus 로고
    • Shelf life of ground beef patties treated by gamma radiation
    • ROBERTS, W. T. and WEEZE, J. O., 1998, Shelf life of ground beef patties treated by gamma radiation. Journal of Food Protein, 61, 1387-1389.
    • (1998) Journal of Food Protein , vol.61 , pp. 1387-1389
    • Roberts, W.T.1    Weeze, J.O.2
  • 38
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • SCHÄGGER, H. and VON JAGOW, G., 1987, Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Analytical Biochemistry, 166, 368-379.
    • (1987) Analytical Biochemistry , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 39
    • 0017915414 scopus 로고
    • Radiation chemistry of amino acids and peptides in aqueous solutions
    • SIMIC, M. G., 1978, Radiation chemistry of amino acids and peptides in aqueous solutions. Journal of Agricultural and Food Chemisty, 26, 6-14.
    • (1978) Journal of Agricultural and Food Chemisty , vol.26 , pp. 6-14
    • Simic, M.G.1
  • 42
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • STOWELL, M. H. B., MCPHILLIPS, T. M., REES, D. C., SOLTIS, S. M., ABRESCH, E. and FEHER, G., 1997, Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science, 276, 812-816.
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 43
    • 0042304501 scopus 로고
    • Radiation chemistry of the liquid states: (2) organic liquids
    • edited by Fahrataziz and M. A. J. Rodgers (New York: WCH Publs)
    • SWALLOW, A. J., 1987, Radiation chemistry of the liquid states: (2) organic liquids. In Radiation Chemistry, Principles and Applications, edited by Fahrataziz and M. A. J. Rodgers (New York: WCH Publs), p. 365.
    • (1987) Radiation Chemistry, Principles and Applications , pp. 365
    • Swallow, A.J.1
  • 44
    • 0022634127 scopus 로고
    • Inactivation of macromolecules by ionizing radiation
    • SWILLENS, S., 1986, Inactivation of macromolecules by ionizing radiation. Biochemical Journal, 233, 655-659.
    • (1986) Biochemical Journal , vol.233 , pp. 655-659
    • Swillens, S.1
  • 48
    • 0032476034 scopus 로고    scopus 로고
    • The active streptococcal hyaluronan synthases (HASs) contain a single HAS monomer and multiple cardiolipin molecules
    • TLAPAK-SIMMONS, V. L., KEMPNER, E. S., BAGGENSTOSS, B. A. and WEIGEL, P. H., 1998, The active streptococcal hyaluronan synthases (HASs) contain a single HAS monomer and multiple cardiolipin molecules. Journal of Biological Chemistry, 273, 26100-26109.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 26100-26109
    • Tlapak-Simmons, V.L.1    Kempner, E.S.2    Baggenstoss, B.A.3    Weigel, P.H.4
  • 49
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • UVERSKY, V. N., 1993, Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry, 32, 13288-13298.
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 51
    • 0021590971 scopus 로고
    • Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetyl-coenzyme-A
    • WIEGAND, G., REMINGTON, S., DEISENHOFER, J. and HUBER, R., 1984, Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetyl-coenzyme-A. Journal of Molecular Biology, 74, 205-219.
    • (1984) Journal of Molecular Biology , vol.74 , pp. 205-219
    • Wiegand, G.1    Remington, S.2    Deisenhofer, J.3    Huber, R.4
  • 52
    • 0030008704 scopus 로고    scopus 로고
    • The effect of free radicals on the conductance induced by alamethicin in planar lipid membranes: Activation and inactivation
    • ZEIDLER, U., WILHELM, M. and STARK, G., 1996, The effect of free radicals on the conductance induced by alamethicin in planar lipid membranes: activation and inactivation. Biochimica Biophysica Acta, 1281, 73-79.
    • (1996) Biochimica Biophysica Acta , vol.1281 , pp. 73-79
    • Zeidler, U.1    Wilhelm, M.2    Stark, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.