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Volumn 1748, Issue 1, 2005, Pages 100-109

A comparison of solution conformation and hydrodynamic properties of equine, porcine and rabbit serum albumin using viscometric measurements

Author keywords

Activation energy; Albumin; Effective specific volume; Huggins coefficient; Hydrodynamic volume; Intrinsic viscosity

Indexed keywords

SERUM ALBUMIN;

EID: 14744293870     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.12.008     Document Type: Article
Times cited : (18)

References (45)
  • 2
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X.M. He, and D.C. Carter Atomic structure and chemistry of human serum albumin Nature 358 1992 209 215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 3
    • 0027219371 scopus 로고
    • X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27-nm resolution
    • J.X. Ho, E.W. Holowachuk, E.J. Norton, P.D. Twigg, and D.C. Carter X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27-nm resolution Eur. J. Biochem. 215 1993 205 212
    • (1993) Eur. J. Biochem. , vol.215 , pp. 205-212
    • Ho, J.X.1    Holowachuk, E.W.2    Norton, E.J.3    Twigg, P.D.4    Carter, D.C.5
  • 4
    • 0032867556 scopus 로고    scopus 로고
    • The three recombinant domains of human serum albumin
    • M. Dockal, D.C. Carter, and F. Rüker The three recombinant domains of human serum albumin J. Biol. Chem. 274 1999 29303 29310
    • (1999) J. Biol. Chem. , vol.274 , pp. 29303-29310
    • Dockal, M.1    Carter, D.C.2    Rüker, F.3
  • 6
    • 0028837623 scopus 로고
    • The subdomain structure of human serum albumin in solution under different pH conditions studied by small angle X-ray scattering
    • J.R. Olivieri, and A.F. Craievich The subdomain structure of human serum albumin in solution under different pH conditions studied by small angle X-ray scattering Eur. Biophys. J. 24 1995 77 84
    • (1995) Eur. Biophys. J. , vol.24 , pp. 77-84
    • Olivieri, J.R.1    Craievich, A.F.2
  • 8
    • 0014382282 scopus 로고
    • The hydrodynamic properties of bovine serum albumin monomer and dimmer
    • P.G. Squire, P. Moser, and C.T. O'Konski The hydrodynamic properties of bovine serum albumin monomer and dimmer Biochemistry 7 1968 4261 4272
    • (1968) Biochemistry , vol.7 , pp. 4261-4272
    • Squire, P.G.1    Moser, P.2    O'Konski, C.T.3
  • 11
    • 0025363484 scopus 로고
    • 2-macroglobulin, fibrinogen, and albumin
    • 2-macroglobulin, fibrinogen, and albumin Biophys. J. 57 1990 389 396
    • (1990) Biophys. J. , vol.57 , pp. 389-396
    • Menon, R.S.1    Allen, P.S.2
  • 12
    • 0027997279 scopus 로고
    • Interparticle interactions and structure in nonideal solutions of human serum albumin studied by small-angle neutron scattering and Monte Carlo simulation
    • B. Sjöberg, and K. Mortensen Interparticle interactions and structure in nonideal solutions of human serum albumin studied by small-angle neutron scattering and Monte Carlo simulation Biophys. Chemist. 52 1994 131 138
    • (1994) Biophys. Chemist. , vol.52 , pp. 131-138
    • Sjöberg, B.1    Mortensen, K.2
  • 13
    • 0030025770 scopus 로고    scopus 로고
    • Viscosity of bovine serum albumin aqueous solutions as a function of temperature and concentration
    • K. Monkos Viscosity of bovine serum albumin aqueous solutions as a function of temperature and concentration Int. J. Biol. Macromol. 18 1996 61 68
    • (1996) Int. J. Biol. Macromol. , vol.18 , pp. 61-68
    • Monkos, K.1
  • 14
    • 0034571042 scopus 로고    scopus 로고
    • Protein interactions with polyelectrolyte multilayers: Interactions between human serum albumin and polystyrene sulfonate/polyallylamine multilayers
    • G. Ladam, C. Gergely, B. Senger, G. Decher, J.-C. Voegel, P. Schaaf, and F.J.G. Cuisinier Protein interactions with polyelectrolyte multilayers: interactions between human serum albumin and polystyrene sulfonate/ polyallylamine multilayers Biomacromolecules 1 2000 674 687
    • (2000) Biomacromolecules , vol.1 , pp. 674-687
    • Ladam, G.1    Gergely, C.2    Senger, B.3    Decher, G.4    Voegel, J.-C.5    Schaaf, P.6    Cuisinier, F.J.G.7
  • 15
    • 0035041251 scopus 로고    scopus 로고
    • The conformation of serum albumin in solution: A combined phosphorescence depolarization-hydrodynamic modeling study
    • M.L. Ferrer, R. Duchowich, B. Carrasco, J. Garcia de la Torre, and A.U. Acuña The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study Biophys. J. 80 2001 2422 2430
    • (2001) Biophys. J. , vol.80 , pp. 2422-2430
    • Ferrer, M.L.1    Duchowich, R.2    Carrasco, B.3    Garcia Delatorre, J.4    Acuña, A.U.5
  • 16
    • 0036160622 scopus 로고    scopus 로고
    • Generalized concentration dependence of globular protein self-diffusion coefficients in aqueous solutions
    • I.V. Nesmelova, V.D. Skirda, and V.D. Fedotov Generalized concentration dependence of globular protein self-diffusion coefficients in aqueous solutions Biopolymers 63 2002 132 140
    • (2002) Biopolymers , vol.63 , pp. 132-140
    • Nesmelova, I.V.1    Skirda, V.D.2    Fedotov, V.D.3
  • 17
    • 2942738911 scopus 로고    scopus 로고
    • On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach
    • K. Monkos On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach Biochim. Biophys. Acta 1700 2004 27 34
    • (2004) Biochim. Biophys. Acta , vol.1700 , pp. 27-34
    • Monkos, K.1
  • 18
    • 0012454921 scopus 로고
    • Electric polarization in proteins - Dielectric dispersion and Kerr effect. Studies of isoionic bovine serum albumin
    • P. Moser, P.G. Squire, and C.T. O'Konski Electric polarization in proteins - dielectric dispersion and Kerr effect. Studies of isoionic bovine serum albumin J. Phys. Chem. 70 1966 744 756
    • (1966) J. Phys. Chem. , vol.70 , pp. 744-756
    • Moser, P.1    Squire, P.G.2    O'Konski, C.T.3
  • 19
    • 1842338655 scopus 로고    scopus 로고
    • Reversible binding interactions between the tryptophan enantiomers and albumins of different animal species as determined by novel high performance liquid chromatographic methods: An attempt to localize the d- and l-tryptophan binding sites on the human serum albumin polypeptide chain by using protein fragments
    • L. Šoltés, and B. Sebille Reversible binding interactions between the tryptophan enantiomers and albumins of different animal species as determined by novel high performance liquid chromatographic methods: an attempt to localize the d- and l-tryptophan binding sites on the human serum albumin polypeptide chain by using protein fragments Chirality 9 1997 373 379
    • (1997) Chirality , vol.9 , pp. 373-379
    • Šoltés, L.1    Sebille, B.2
  • 20
    • 0031758949 scopus 로고    scopus 로고
    • An electrophoretic study on interactions of albumins of different species with immobilized Cibacron Blue F3G a
    • I. Miller, and M. Gemeiner An electrophoretic study on interactions of albumins of different species with immobilized Cibacron Blue F3G A Electrophoresis 19 1998 2506 2514
    • (1998) Electrophoresis , vol.19 , pp. 2506-2514
    • Miller, I.1    Gemeiner, M.2
  • 21
    • 0034643906 scopus 로고    scopus 로고
    • Interaction of albumins from different species with phospholipids liposomes. Multiple binding sites system
    • M.N. Dimitrova, H. Matsumura, A. Dimitrova, and V.Z. Neitchev Interaction of albumins from different species with phospholipids liposomes. Multiple binding sites system Int. J. Biol. Macromol. 27 2000 187 194
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 187-194
    • Dimitrova, M.N.1    Matsumura, H.2    Dimitrova, A.3    Neitchev, V.Z.4
  • 22
    • 0035437692 scopus 로고    scopus 로고
    • Effect of sugars on rabbit serum albumin stability and induction of secondary structure
    • R.H. Khan, and M.S. Shabnum Effect of sugars on rabbit serum albumin stability and induction of secondary structure Biochemistry (Moscow) 66 2001 1280 1285
    • (2001) Biochemistry (Moscow) , vol.66 , pp. 1280-1285
    • Khan, R.H.1    Shabnum, M.S.2
  • 23
    • 0037203854 scopus 로고    scopus 로고
    • Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: Spectroscopy and modelling
    • E.L. Gelamo, C.H.T.P. Silva, H. Imasato, and M. Tabak Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling Biochim. Biophys. Acta 1594 2002 84 99
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 84-99
    • Gelamo, E.L.1    Silva, C.H.T.P.2    Imasato, H.3    Tabak, M.4
  • 24
    • 0010962165 scopus 로고
    • Über die berechnung der gestalt von proteinmolekülen
    • A. Polson Über die berechnung der gestalt von proteinmolekülen Kolloid-Z. 88 1939 51 61
    • (1939) Kolloid-Z. , vol.88 , pp. 51-61
    • Polson, A.1
  • 25
    • 0026409260 scopus 로고
    • Determination of the axial ratio of globular proteins in aqueous solution using viscometric measurements
    • K. Monkos, and B. Turczynski Determination of the axial ratio of globular proteins in aqueous solution using viscometric measurements Int. J. Biol. Macromol. 13 1991 341 344
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 341-344
    • Monkos, K.1    Turczynski, B.2
  • 26
    • 0004212461 scopus 로고
    • Viscosity-temperature relationships for polymers in bulk
    • F.R. Eirich Academic Press New York
    • T.G. Fox, S. Gratch, and S. Loshaek F.R. Eirich Viscosity-temperature relationships for polymers in bulk Rheology. theory and applications vol. 1 1956 Academic Press New York 447 457
    • (1956) Rheology. Theory and Applications , vol.1 , pp. 447-457
    • Fox, T.G.1    Gratch, S.2    Loshaek, S.3
  • 28
    • 0030947242 scopus 로고    scopus 로고
    • Concentration and temperature dependence of viscosity in lysozyme aqueous solutions
    • K. Monkos Concentration and temperature dependence of viscosity in lysozyme aqueous solutions Biochim. Biophys. Acta 1339 1997 304 310
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 304-310
    • Monkos, K.1
  • 29
    • 0032819751 scopus 로고    scopus 로고
    • A comparative study on viscosity of human, bovine and pig IgG immunoglobulins in aqueous solutions
    • K. Monkos, and B. Turczynski A comparative study on viscosity of human, bovine and pig IgG immunoglobulins in aqueous solutions Int. J. Biol. Macromol. 26 1999 155 159
    • (1999) Int. J. Biol. Macromol. , vol.26 , pp. 155-159
    • Monkos, K.1    Turczynski, B.2
  • 30
    • 0034737923 scopus 로고    scopus 로고
    • Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin
    • K. Monkos Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin Biophys. Chemist. 85 2000 7 16
    • (2000) Biophys. Chemist. , vol.85 , pp. 7-16
    • Monkos, K.1
  • 31
    • 0028184696 scopus 로고
    • Microwave dielectric study on bound water of globule proteins in aqueous solution
    • N. Miura, N. Asaka, N. Shinyashiki, and S. Mashimo Microwave dielectric study on bound water of globule proteins in aqueous solution Biopolymers 34 1994 357 364
    • (1994) Biopolymers , vol.34 , pp. 357-364
    • Miura, N.1    Asaka, N.2    Shinyashiki, N.3    Mashimo, S.4
  • 32
    • 0035924848 scopus 로고    scopus 로고
    • Hydration study of globular proteins by microwave dielectric spectroscopy
    • K. Yokoyama, T. Kamei, H. Minami, and M. Suzuki Hydration study of globular proteins by microwave dielectric spectroscopy J. Phys. Chem., B 105 2001 12622 12627
    • (2001) J. Phys. Chem., B , vol.105 , pp. 12622-12627
    • Yokoyama, K.1    Kamei, T.2    Minami, H.3    Suzuki, M.4
  • 34
    • 0031554728 scopus 로고    scopus 로고
    • The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution
    • S.E. Harding The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution Prog. Biophys. Mol. Biol. 68 1997 207 262
    • (1997) Prog. Biophys. Mol. Biol. , vol.68 , pp. 207-262
    • Harding, S.E.1
  • 35
    • 0027957802 scopus 로고
    • A study of the molecular sources of nonideal osmotic pressure of bovine serum albumin solutions as a function of pH
    • K.M. Kanal, G.D. Fullerton, and I.L. Cameron A study of the molecular sources of nonideal osmotic pressure of bovine serum albumin solutions as a function of pH Biophys. J. 66 1994 153 160
    • (1994) Biophys. J. , vol.66 , pp. 153-160
    • Kanal, K.M.1    Fullerton, G.D.2    Cameron, I.L.3
  • 36
    • 0029100915 scopus 로고
    • Computation of the dipole moment of proteins
    • J. Antosiewicz Computation of the dipole moment of proteins Biophys. J. 69 1995 1344 1354
    • (1995) Biophys. J. , vol.69 , pp. 1344-1354
    • Antosiewicz, J.1
  • 37
    • 0035119340 scopus 로고    scopus 로고
    • The structure and dipole moment of globular proteins in solution and crystalline states: Use of NMR and X-ray databases for the numerical calculation of dipole moment
    • S. Takashima The structure and dipole moment of globular proteins in solution and crystalline states: use of NMR and X-ray databases for the numerical calculation of dipole moment Biopolymers 58 2001 398 409
    • (2001) Biopolymers , vol.58 , pp. 398-409
    • Takashima, S.1
  • 38
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • S.B. Zimmerman, and S.O. Trach Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli J. Mol. Biol. 222 1991 599 620
    • (1991) J. Mol. Biol. , vol.222 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2
  • 39
    • 0002278843 scopus 로고
    • Scaled particle methods in the statistical thermodynamics of fluids
    • H. Reiss Scaled particle methods in the statistical thermodynamics of fluids Adv. Chem. Phys. 9 1965 1 84
    • (1965) Adv. Chem. Phys. , vol.9 , pp. 1-84
    • Reiss, H.1
  • 40
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • S.B. Zimmerman, and A.P. Minton Macromolecular crowding: biochemical, biophysical, and physiological consequences Annu. Rev. Biophys. Biomol. Struct. 22 1993 27 65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 41
    • 34249290252 scopus 로고
    • The viscosity of a concentrated suspension of spherical particles
    • M.J. Mooney The viscosity of a concentrated suspension of spherical particles J. Colloid Sci. 6 1951 162 170
    • (1951) J. Colloid Sci. , vol.6 , pp. 162-170
    • Mooney, M.J.1
  • 42
    • 0002276429 scopus 로고
    • The influence of Brownian movement on the viscosity of solutions
    • R. Simha The influence of Brownian movement on the viscosity of solutions J. Phys. Chem. 44 1940 25 34
    • (1940) J. Phys. Chem. , vol.44 , pp. 25-34
    • Simha, R.1
  • 43
    • 14744301887 scopus 로고    scopus 로고
    • Viscosity-temperature dependence for human gamma-globulin aqueous solutions at a wide range of concentrations
    • K. Monkos, and B. Turczynski Viscosity-temperature dependence for human gamma-globulin aqueous solutions at a wide range of concentrations Curr. Top. Biophys. 21 1997 113 116
    • (1997) Curr. Top. Biophys. , vol.21 , pp. 113-116
    • Monkos, K.1    Turczynski, B.2
  • 44
    • 0000069429 scopus 로고
    • Huggins coefficient for the viscosity of polymer solutions
    • K.F. Freed, and S.F. Edwards Huggins coefficient for the viscosity of polymer solutions J. Chem. Phys. 62 1975 4032 4035
    • (1975) J. Chem. Phys. , vol.62 , pp. 4032-4035
    • Freed, K.F.1    Edwards, S.F.2


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