Thermochemical, volumetric and spectroscopic properties of lysozyme-poly(ethylene) glycol system (214 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2006; 83(3): 587-595.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.438, 5-year impact factor: 1.908
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33645679043&partnerID=40&md5=330316ab42c990447d40c93f6ae7b080
Keywords: Density, Fluorescence Intensity, Lysozyme Unfolding, Macromolecular Crowding, Peg, Preferential Hydration, Acoustic Impedance, Enthalpy, Permittivity, Polyethylene Glycols, Enzymes,
Affiliations:
*** IBB - CNR ***
Institute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224 Warsaw, Poland
Institute for Macromolecular Studies, Division of Genova, CNR, Via De Marini 6, 16-149 Genova, Italy
References:
Middaugh, C.R., Tisel, W.A., Haire, R.N., Rosenberg, A., (1978) J. Biol. Chem., 254, p. 36
Laurent, T.C., (1971) Eur. J. Biochem., 21, p. 498
Harris, J.M., (1992) Poly(Ethylene Glycol) Chemistry: Biotechnical and Biomedical Applications, , Plenum Press, New York
Verheyen, S., Blaton, N., Kinget, R., Van Den Mooter, G., (2004) J. Therm. Anal. Cal., 76, p. 405
Zimmerman, S.B., Minton, A.P., (1993) Annu. Rev. Biomol. Struct., 22, p. 27
Ellis, R.J., Minton, A.P., (2003) Nature, 425, p. 27
Ellis, R.J., (2001) Trends in Biochem. Sci., 26, p. 597
Lee, L.L.-Y., Lee, J.C., (1987) Biochemistry, 26, p. 7831
Malzert, A., Boury, F., Renard, D., Robert, P., Lavenant, L., Benoit, J.P., Proust, J.E., (2003) Int. J. Pharm., 260, p. 175
Knoll, D.A., Hermans, J., (1981) Biopolymers, 20, p. 1747
Atha, D.H., Ingham, K.C., (1981) J. Biol. Chem., 256, p. 12108
Sasahara, K., McPhe, P., Minton, A.P., (2003) J. Mol. Biol., 326, p. 1227
Ferruggia, B., Nerli, B., Di Nuci, H., Rigatusso, R., Pico, G., (1999) Int. J. Biol. Macromol, 26, p. 23
Privalov, P.L., Potekhin, S.A., (1986) Methods Enzymol., 131, p. 4
Shnyrov, V.L., Sanchez-Ruiz, J.M., Boiko, B.N., Zhadan, G.G., Permyakov, E.A., (1997) Thermochim. Acta, 302, p. 165
Privalov, P.L., Khechinashvili, N.N., (1974) J. Mol. Biol., 86, p. 665
Pfeil, W., Privalov, P.L., (1976) Biophys. Chem., 4, p. 23
Privalov, P.L., Makhatadze, G.I., (1990) J. Mol. Biol., 213, p. 385
Plotnikov, V.V., Brandts, J.M., Lin, L.N., Brandts, J.F., (1997) Anal. Biochem., 250, p. 237
Michnik, A., Kołos, A., Drzazga, Z., (2004) J. Therm. Anal. Cal., 77, p. 269
Hinz, H.J., Schwarz, F.P., (2001) Pure Appl. Chem. (IUPAC), 73, p. 745
Arnold, K., Hermann, A., Pratsch, L., Gawrisch, K., (1985) BBA, 815, p. 515
Mateo, P.L., Differental scanning calorimetry applications to protein solutions (1984) Thermochemistry and Its Applications to Chemical and Biochemical Systems, pp. 341-368
Robertson, A.D., Murphy, K.P., (1997) Chem. Rev., 97, p. 1251
Timasheff, S.N., Fasman, G.D., (1969) Structure and Stability of Biological Macromolecules, , Marcel Dekker Inc., New York
Timasheff, S.N., (1993) Annu. Rev. Biophys. Biomol. Struct., 22, p. 67
Chalikian, T.V., (2003) Annu. Rev. Biophys. Biomol. Struct., 32, p. 207
Sophianopoulos, A.J., Rhode, C.K.J., Holcomb, D.N., Van Holde, K.E., (1962) J. Biol. Chem., 237, p. 1107
Tanford, C., (1961) Physical Chemistry of Macromolecules, , J. Wiley, New York
Creighton, T.E., (1992) Proteins: Structure and Molecular Properties, , W. H. Freeman and company, New York
Cao, A., Wang, G., Tang, Y., Lai, L., (2002) Biochem. Biophys. Res. Com., 291, p. 795
Hirai, M., Arai, S., Iwase, H., Takizawa, T., (1998) J. Phys. Chem. B, 102, p. 1308
Hermans, J., (1982) J. Chem. Phys., 77, p. 2193
Middaugh, C. R., Tisel, W. A., Haire, R. N., Rosenberg, A., (1978) J. Biol. Chem., 254, p. 36
Laurent, T. C., (1971) Eur. J. Biochem., 21, p. 498
Harris, J. M., (1992) Poly (Ethylene Glycol) Chemistry: Biotechnical and Biomedical Applications, , Plenum Press, New York
Zimmerman, S. B., Minton, A. P., (1993) Annu. Rev. Biomol. Struct., 22, p. 27
Ellis, R. J., Minton, A. P., (2003) Nature, 425, p. 27
Ellis, R. J., (2001) Trends in Biochem. Sci., 26, p. 597
Lee, L. L. -Y., Lee, J. C., (1987) Biochemistry, 26, p. 7831
Knoll, D. A., Hermans, J., (1981) Biopolymers, 20, p. 1747
Atha, D. H., Ingham, K. C., (1981) J. Biol. Chem., 256, p. 12108
Privalov, P. L., Potekhin, S. A., (1986) Methods Enzymol., 131, p. 4
Shnyrov, V. L., Sanchez-Ruiz, J. M., Boiko, B. N., Zhadan, G. G., Permyakov, E. A., (1997) Thermochim. Acta, 302, p. 165
Privalov, P. L., Khechinashvili, N. N., (1974) J. Mol. Biol., 86, p. 665
Privalov, P. L., Makhatadze, G. I., (1990) J. Mol. Biol., 213, p. 385
Plotnikov, V. V., Brandts, J. M., Lin, L. N., Brandts, J. F., (1997) Anal. Biochem., 250, p. 237
Michnik, A., Ko os, A., Drzazga, Z., (2004) J. Therm. Anal. Cal., 77, p. 269
Hinz, H. J., Schwarz, F. P., (2001) Pure Appl. Chem. (IUPAC), 73, p. 745
Mateo, P. L., Differental scanning calorimetry applications to protein solutions (1984) Thermochemistry and Its Applications to Chemical and Biochemical Systems, pp. 341-368
Robertson, A. D., Murphy, K. P., (1997) Chem. Rev., 97, p. 1251
Timasheff, S. N., Fasman, G. D., (1969) Structure and Stability of Biological Macromolecules, , Marcel Dekker Inc., New York
Timasheff, S. N., (1993) Annu. Rev. Biophys. Biomol. Struct., 22, p. 67
Chalikian, T. V., (2003) Annu. Rev. Biophys. Biomol. Struct., 32, p. 207
Sophianopoulos, A. J., Rhode, C. K. J., Holcomb, D. N., Van Holde, K. E., (1962) J. Biol. Chem., 237, p. 1107
Creighton, T. E., (1992) Proteins: Structure and Molecular Properties, , W. H. Freeman and company, New York
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2006; 83(3): 587-595.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.438, 5-year impact factor: 1.908
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33645679043&partnerID=40&md5=330316ab42c990447d40c93f6ae7b080
Keywords: Density, Fluorescence Intensity, Lysozyme Unfolding, Macromolecular Crowding, Peg, Preferential Hydration, Acoustic Impedance, Enthalpy, Permittivity, Polyethylene Glycols, Enzymes,
Affiliations:
*** IBB - CNR ***
Institute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, 01-224 Warsaw, Poland
Institute for Macromolecular Studies, Division of Genova, CNR, Via De Marini 6, 16-149 Genova, Italy
References:
Middaugh, C.R., Tisel, W.A., Haire, R.N., Rosenberg, A., (1978) J. Biol. Chem., 254, p. 36
Laurent, T.C., (1971) Eur. J. Biochem., 21, p. 498
Harris, J.M., (1992) Poly(Ethylene Glycol) Chemistry: Biotechnical and Biomedical Applications, , Plenum Press, New York
Verheyen, S., Blaton, N., Kinget, R., Van Den Mooter, G., (2004) J. Therm. Anal. Cal., 76, p. 405
Zimmerman, S.B., Minton, A.P., (1993) Annu. Rev. Biomol. Struct., 22, p. 27
Ellis, R.J., Minton, A.P., (2003) Nature, 425, p. 27
Ellis, R.J., (2001) Trends in Biochem. Sci., 26, p. 597
Lee, L.L.-Y., Lee, J.C., (1987) Biochemistry, 26, p. 7831
Malzert, A., Boury, F., Renard, D., Robert, P., Lavenant, L., Benoit, J.P., Proust, J.E., (2003) Int. J. Pharm., 260, p. 175
Knoll, D.A., Hermans, J., (1981) Biopolymers, 20, p. 1747
Atha, D.H., Ingham, K.C., (1981) J. Biol. Chem., 256, p. 12108
Sasahara, K., McPhe, P., Minton, A.P., (2003) J. Mol. Biol., 326, p. 1227
Ferruggia, B., Nerli, B., Di Nuci, H., Rigatusso, R., Pico, G., (1999) Int. J. Biol. Macromol, 26, p. 23
Privalov, P.L., Potekhin, S.A., (1986) Methods Enzymol., 131, p. 4
Shnyrov, V.L., Sanchez-Ruiz, J.M., Boiko, B.N., Zhadan, G.G., Permyakov, E.A., (1997) Thermochim. Acta, 302, p. 165
Privalov, P.L., Khechinashvili, N.N., (1974) J. Mol. Biol., 86, p. 665
Pfeil, W., Privalov, P.L., (1976) Biophys. Chem., 4, p. 23
Privalov, P.L., Makhatadze, G.I., (1990) J. Mol. Biol., 213, p. 385
Plotnikov, V.V., Brandts, J.M., Lin, L.N., Brandts, J.F., (1997) Anal. Biochem., 250, p. 237
Michnik, A., Kołos, A., Drzazga, Z., (2004) J. Therm. Anal. Cal., 77, p. 269
Hinz, H.J., Schwarz, F.P., (2001) Pure Appl. Chem. (IUPAC), 73, p. 745
Arnold, K., Hermann, A., Pratsch, L., Gawrisch, K., (1985) BBA, 815, p. 515
Mateo, P.L., Differental scanning calorimetry applications to protein solutions (1984) Thermochemistry and Its Applications to Chemical and Biochemical Systems, pp. 341-368
Robertson, A.D., Murphy, K.P., (1997) Chem. Rev., 97, p. 1251
Timasheff, S.N., Fasman, G.D., (1969) Structure and Stability of Biological Macromolecules, , Marcel Dekker Inc., New York
Timasheff, S.N., (1993) Annu. Rev. Biophys. Biomol. Struct., 22, p. 67
Chalikian, T.V., (2003) Annu. Rev. Biophys. Biomol. Struct., 32, p. 207
Sophianopoulos, A.J., Rhode, C.K.J., Holcomb, D.N., Van Holde, K.E., (1962) J. Biol. Chem., 237, p. 1107
Tanford, C., (1961) Physical Chemistry of Macromolecules, , J. Wiley, New York
Creighton, T.E., (1992) Proteins: Structure and Molecular Properties, , W. H. Freeman and company, New York
Cao, A., Wang, G., Tang, Y., Lai, L., (2002) Biochem. Biophys. Res. Com., 291, p. 795
Hirai, M., Arai, S., Iwase, H., Takizawa, T., (1998) J. Phys. Chem. B, 102, p. 1308
Hermans, J., (1982) J. Chem. Phys., 77, p. 2193
Middaugh, C. R., Tisel, W. A., Haire, R. N., Rosenberg, A., (1978) J. Biol. Chem., 254, p. 36
Laurent, T. C., (1971) Eur. J. Biochem., 21, p. 498
Harris, J. M., (1992) Poly (Ethylene Glycol) Chemistry: Biotechnical and Biomedical Applications, , Plenum Press, New York
Zimmerman, S. B., Minton, A. P., (1993) Annu. Rev. Biomol. Struct., 22, p. 27
Ellis, R. J., Minton, A. P., (2003) Nature, 425, p. 27
Ellis, R. J., (2001) Trends in Biochem. Sci., 26, p. 597
Lee, L. L. -Y., Lee, J. C., (1987) Biochemistry, 26, p. 7831
Knoll, D. A., Hermans, J., (1981) Biopolymers, 20, p. 1747
Atha, D. H., Ingham, K. C., (1981) J. Biol. Chem., 256, p. 12108
Privalov, P. L., Potekhin, S. A., (1986) Methods Enzymol., 131, p. 4
Shnyrov, V. L., Sanchez-Ruiz, J. M., Boiko, B. N., Zhadan, G. G., Permyakov, E. A., (1997) Thermochim. Acta, 302, p. 165
Privalov, P. L., Khechinashvili, N. N., (1974) J. Mol. Biol., 86, p. 665
Privalov, P. L., Makhatadze, G. I., (1990) J. Mol. Biol., 213, p. 385
Plotnikov, V. V., Brandts, J. M., Lin, L. N., Brandts, J. F., (1997) Anal. Biochem., 250, p. 237
Michnik, A., Ko os, A., Drzazga, Z., (2004) J. Therm. Anal. Cal., 77, p. 269
Hinz, H. J., Schwarz, F. P., (2001) Pure Appl. Chem. (IUPAC), 73, p. 745
Mateo, P. L., Differental scanning calorimetry applications to protein solutions (1984) Thermochemistry and Its Applications to Chemical and Biochemical Systems, pp. 341-368
Robertson, A. D., Murphy, K. P., (1997) Chem. Rev., 97, p. 1251
Timasheff, S. N., Fasman, G. D., (1969) Structure and Stability of Biological Macromolecules, , Marcel Dekker Inc., New York
Timasheff, S. N., (1993) Annu. Rev. Biophys. Biomol. Struct., 22, p. 67
Chalikian, T. V., (2003) Annu. Rev. Biophys. Biomol. Struct., 32, p. 207
Sophianopoulos, A. J., Rhode, C. K. J., Holcomb, D. N., Van Holde, K. E., (1962) J. Biol. Chem., 237, p. 1107
Creighton, T. E., (1992) Proteins: Structure and Molecular Properties, , W. H. Freeman and company, New York
Thermochemical, volumetric and spectroscopic properties of lysozyme-poly(ethylene) glycol system
Investigations of lysozyme-polyethylene glycol system were made by differential scanning calorimetry, fluorescence and density techniques. The values of unfolding enthalpies, ΔH N U, unfolding temperatures, T m, excess molar heat capacities, ΔC p, and apparent molar volumes, V Φ , were determined as functions of PEG concentration. The three PEGs of average molecular mass (MW) 6000, 10000, 20000 were used as macromolecular crowding agents. The concentration of polymers was changed in the range 0-30% mass per volume (w/v). The values of ΔH N U remained constant with no dependence on PEG concentration, while PEG addition to buffered lysozyme solutions caused linear decrease of T m. The values of ΔC p and V Φ of lysozyme dramatically changed in the range of 8-10% of PEG concentration. The fluorescence spectroscopy was used in order to investigate the polymer influence on possible solvent-lysozyme interactions. The electrical properties of polymer-water and polymer-buffer systems, the dielectric constants of solutions were determined with use of impedance spectroscopy. © 2006 Akadémiai Kiadó.
Investigations of lysozyme-polyethylene glycol system were made by differential scanning calorimetry, fluorescence and density techniques. The values of unfolding enthalpies, ΔH N U, unfolding temperatures, T m, excess molar heat capacities, ΔC p, and apparent molar volumes, V Φ , were determined as functions of PEG concentration. The three PEGs of average molecular mass (MW) 6000, 10000, 20000 were used as macromolecular crowding agents. The concentration of polymers was changed in the range 0-30% mass per volume (w/v). The values of ΔH N U remained constant with no dependence on PEG concentration, while PEG addition to buffered lysozyme solutions caused linear decrease of T m. The values of ΔC p and V Φ of lysozyme dramatically changed in the range of 8-10% of PEG concentration. The fluorescence spectroscopy was used in order to investigate the polymer influence on possible solvent-lysozyme interactions. The electrical properties of polymer-water and polymer-buffer systems, the dielectric constants of solutions were determined with use of impedance spectroscopy. © 2006 Akadémiai Kiadó.
Thermochemical, volumetric and spectroscopic properties of lysozyme-poly(ethylene) glycol system
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Thermochemical, volumetric and spectroscopic properties of lysozyme-poly(ethylene) glycol system
Other filter: ([btitle,keywords] "Fluorescence Intensi ...
Vergara A, Capuano F, Paduano L, Sartorio R
* Lysozyme mutual diffusion in solutions crowded by poly(ethylene glycol) (226 views)
Macromolecules (ISSN: 0024-9297), 2006; 39(13): 4500-4506.
Impact Factor: 4.277
View Export to BibTeX Export to EndNote
* Lysozyme mutual diffusion in solutions crowded by poly(ethylene glycol) (226 views)
Macromolecules (ISSN: 0024-9297), 2006; 39(13): 4500-4506.
Impact Factor: 4.277
View Export to BibTeX Export to EndNote
1 Records (1 excluding Abstracts).
Total impact factor: 4.277 (4.277 excluding Abstracts).
Total 5 year impact factor: 5.531 (5.531 excluding Abstracts).
Total impact factor: 4.277 (4.277 excluding Abstracts).
Total 5 year impact factor: 5.531 (5.531 excluding Abstracts).
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