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Volumn 36, Issue 7, 2007, Pages 717-725

Thermal aggregation of bovine serum albumin at different pH: Comparison with human serum albumin

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE SERUM ALBUMIN; DYE; HUMAN SERUM ALBUMIN; TRYPTOPHAN;

EID: 35748957119     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-007-0196-5     Document Type: Conference Paper
Times cited : (106)

References (48)
  • 1
    • 0032995379 scopus 로고    scopus 로고
    • Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle X-ray scattering
    • Arai S, Hirai M (1999) Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle X-ray scattering. Biophys J 76:2192-2197
    • (1999) Biophys J , vol.76 , pp. 2192-2197
    • Arai, S.1    Hirai, M.2
  • 2
    • 0033855656 scopus 로고    scopus 로고
    • Immunoglobulin light chain amyloidoses: The archetype of structural and pathogenic variability
    • Bellotti V, Mangione P, Merlini G (2000) Immunoglobulin light chain amyloidoses: the archetype of structural and pathogenic variability. J Struct Biol 130:280-289
    • (2000) J Struct Biol , vol.130 , pp. 280-289
    • Bellotti, V.1    Mangione, P.2    Merlini, G.3
  • 3
    • 26444569477 scopus 로고    scopus 로고
    • Probing BSA binding to citrate-coated gold nanoparticles and surfaces
    • 20
    • Brewer SH, Glomm WR, Johnson MC, Knag MK, Franzen S (2005) Probing BSA binding to citrate-coated gold nanoparticles and surfaces. Langmuir 21(20):9303-9307
    • (2005) Langmuir , vol.21 , pp. 9303-9307
    • Brewer, S.H.1    Glomm, W.R.2    Johnson, M.C.3    Knag, M.K.4    Franzen, S.5
  • 5
    • 28444454101 scopus 로고    scopus 로고
    • Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    • Calamai M, Chiti F, Dobson CM (2005) Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys J 89:4201-4210
    • (2005) Biophys J , vol.89 , pp. 4201-4210
    • Calamai, M.1    Chiti, F.2    Dobson, C.M.3
  • 6
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter DC, Ho JX (1994) Structure of serum albumin. Adv Protein Chem 45:153-203
    • (1994) Adv Protein Chem , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 7
    • 0002121327 scopus 로고
    • Stochastic problems in physics and astronomy
    • Chandrasekhar S (1943) Stochastic problems in physics and astronomy. Rev Mod Phys 15:1-89
    • (1943) Rev Mod Phys , vol.15 , pp. 1-89
    • Chandrasekhar, S.1
  • 9
    • 0033049201 scopus 로고    scopus 로고
    • Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to β-lactolgobulin from fluorescence spectroscopy
    • D'Alfonso L, Collini M, Baldini G (1999) Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to β-lactolgobulin from fluorescence spectroscopy. Biochimica et Biophysica Acta 1432:194-202
    • (1999) Biochimica et Biophysica Acta , vol.1432 , pp. 194-202
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 10
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426:884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 11
    • 0034602966 scopus 로고    scopus 로고
    • Conformational transitions of the three recombinant domains of human serum albumin depending on pH
    • Dockal M, Carter DC, Rüker F (2000) Conformational transitions of the three recombinant domains of human serum albumin depending on pH. J Biol Chem 275:3042-3050
    • (2000) J Biol Chem , vol.275 , pp. 3042-3050
    • Dockal, M.1    Carter, D.C.2    Rüker, F.3
  • 15
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F (1999) Analysis of protein aggregation kinetics. Methods Enzymol 309:256-274
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 17
    • 0001851995 scopus 로고
    • Rosenoer VM, Oratz M, Rothschield MA (eds) Pregamon Press, Oxford
    • Foster JF (1977) In: Rosenoer VM, Oratz M, Rothschield MA (eds) Albumin structure, function and uses. Pregamon Press, Oxford, pp 53-84
    • (1977) Albumin Structure, Function and Uses , pp. 53-84
    • Foster, J.F.1
  • 18
    • 0037203854 scopus 로고    scopus 로고
    • Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: Spectroscopy and modelling
    • 1
    • Gelamo EL, Silva CH, Imasato H, Tabak M (2002) Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling. Biochim Biophys Acta 1594(1):84-99
    • (2002) Biochim Biophys Acta , vol.1594 , pp. 84-99
    • Gelamo, E.L.1    Silva, C.H.2    Imasato, H.3    Tabak, M.4
  • 20
    • 0001425703 scopus 로고
    • The availability of the disulfide bonds of human and bovine serum albumin and of bovine gamma-globulin to reduction by thioglycolic acid
    • Katchalski E, Benjamin GS, Gross V (1957) The availability of the disulfide bonds of human and bovine serum albumin and of bovine gamma-globulin to reduction by thioglycolic acid. J Am Chem Soc 79:4096-4099
    • (1957) J Am Chem Soc , vol.79 , pp. 4096-4099
    • Katchalski, E.1    Benjamin, G.S.2    Gross, V.3
  • 21
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly JW (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struc Biol 8:101-106
    • (1998) Curr Opin Struc Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 24
    • 22244456042 scopus 로고    scopus 로고
    • Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy
    • 6
    • Lindgren M, Sorgjerd K, Hammarstrom P (2005) Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy. Biophys J 88(6):4200-12
    • (2005) Biophys J , vol.88 , pp. 4200-12
    • Lindgren, M.1    Sorgjerd, K.2    Hammarstrom, P.3
  • 26
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • Militello V, Casarino C, Emanuele A, Giostra A, Pullara F, Leone M (2004) Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys Chem 107:175-187
    • (2004) Biophys Chem , vol.107 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 27
    • 0043161935 scopus 로고    scopus 로고
    • Conformational changes involved in thermal aggregation processes of bovine serum albumin
    • Militello V, Vetri V, Leone M (2003) Conformational changes involved in thermal aggregation processes of bovine serum albumin. Biophys Chem 105:133-141
    • (2003) Biophys Chem , vol.105 , pp. 133-141
    • Militello, V.1    Vetri, V.2    Leone, M.3
  • 28
    • 30744477442 scopus 로고    scopus 로고
    • Single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: Analysis of the early stages of fibril formation
    • 2
    • Morel B, Casares S, Conejero-Lara FA (2006) Single mutation induces amyloid aggregation in the alpha-spectrin SH3 domain: analysis of the early stages of fibril formation. J Mol Biol 356(2):453-68
    • (2006) J Mol Biol , vol.356 , pp. 453-68
    • Morel, B.1    Casares, S.2    Conejero-Lara, F.A.3
  • 29
    • 0029924912 scopus 로고    scopus 로고
    • Fluorescence behaviour of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: A comparative study of the two and one tryptophan(s) of bovine and human albumins
    • Moriyama Y, Ohta D, Hachiya K, Mitsui Y, Takeda K (1996) Fluorescence behaviour of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins. J Prot Chem 15:265-271
    • (1996) J Prot Chem , vol.15 , pp. 265-271
    • Moriyama, Y.1    Ohta, D.2    Hachiya, K.3    Mitsui, Y.4    Takeda, K.5
  • 30
    • 1542533563 scopus 로고    scopus 로고
    • Role of protein-water interactions and electrostatics in (α-synuclein fibril formation
    • Munishkina LA, Henriques J, Uversky VN, Fink AL (2004) Role of protein-water interactions and electrostatics in (α-synuclein fibril formation. Biochemistry 43:3289-3300
    • (2004) Biochemistry , vol.43 , pp. 3289-3300
    • Munishkina, L.A.1    Henriques, J.2    Uversky, V.N.3    Fink, A.L.4
  • 31
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibrils formation
    • Naiki H, Gejyo F (1999) Kinetic analysis of amyloid fibrils formation. Methods Enzym 309:305-318
    • (1999) Methods Enzym , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 32
    • 0030829751 scopus 로고    scopus 로고
    • Conformational changes in seventeen cysteine disulfide bridges of bovine serum albumin proved by Raman spectroscopy
    • 3
    • Nakamura K, Era S, Ozaki Y, Sogami M, Hayashi T, Murakami M (1997) Conformational changes in seventeen cysteine disulfide bridges of bovine serum albumin proved by Raman spectroscopy. FEBS Lett 417(3):375-8
    • (1997) FEBS Lett , vol.417 , pp. 375-8
    • Nakamura, K.1    Era, S.2    Ozaki, Y.3    Sogami, M.4    Hayashi, T.5    Murakami, M.6
  • 33
    • 0037019837 scopus 로고    scopus 로고
    • Electrochemical behaviour of human serum albumin-TiO2 nanocrystalline electrodes studied as a function of pH, part 1: Voltammetric response
    • 1
    • Oliva FY, Avalle LB, Camara OR (2002) Electrochemical behaviour of human serum albumin-TiO2 nanocrystalline electrodes studied as a function of pH, part 1: voltammetric response. J Electroanal Chem 534(1):19-29
    • (2002) J Electroanal Chem , vol.534 , pp. 19-29
    • Oliva, F.Y.1    Avalle, L.B.2    Camara, O.R.3
  • 36
    • 0027417602 scopus 로고
    • PH-induced structural transitions of bovine serum albumin: Histidine pKa values and unfolding of the N-terminus during the N to F transition
    • Sadler PJ, Tucker A (1993) pH-induced structural transitions of bovine serum albumin: histidine pKa values and unfolding of the N-terminus during the N to F transition. Eur J Biochem 212:811-817
    • (1993) Eur J Biochem , vol.212 , pp. 811-817
    • Sadler, P.J.1    Tucker, A.2
  • 39
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • 11
    • Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81(11):678-699
    • (2003) J Mol Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 40
    • 33751285404 scopus 로고    scopus 로고
    • Amyloid fibril formation and other aggregate species formed by human serum albumin association
    • 42
    • Taboada P, Barbosa S, Castro E, Mosquera V (2006) Amyloid fibril formation and other aggregate species formed by human serum albumin association. J Phys Chem B 110(42):20733-20736
    • (2006) J Phys Chem B , vol.110 , pp. 20733-20736
    • Taboada, P.1    Barbosa, S.2    Castro, E.3    Mosquera, V.4
  • 41
    • 2542606804 scopus 로고    scopus 로고
    • Effects of the molecular structure of two amphiphilic antidepressant drugs on the formation of complexes with human serum albumin.
    • 3
    • Taboada P, Gutierrez-Pichel M, Mosquera V (2004) Effects of the molecular structure of two amphiphilic antidepressant drugs on the formation of complexes with human serum albumin. Biomacromolecules 5(3):1116-1123
    • (2004) Biomacromolecules , vol.5 , pp. 1116-1123
    • Taboada, P.1    Gutierrez-Pichel, M.2    Mosquera, V.3
  • 42
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded.
    • 2
    • Uversky VN, Fink AL (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698(2):131-53
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-53
    • Uversky, V.N.1    Fink, A.L.2
  • 44
    • 11144317965 scopus 로고    scopus 로고
    • Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin
    • Vetri V, Militello V (2005) Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin. Biophys Chem 13:83-91
    • (2005) Biophys Chem , vol.13 , pp. 83-91
    • Vetri, V.1    Militello, V.2
  • 46
    • 0034518920 scopus 로고    scopus 로고
    • Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin sub-domain in the presence of guanidine hydrochloride
    • Viallet M, Vo-Dinh PT, Ribou AC, Vigo J, Salmon JM (2000) Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin sub-domain in the presence of guanidine hydrochloride. J Prot Chem 19:431-438
    • (2000) J Prot Chem , vol.19 , pp. 431-438
    • Viallet, M.1    Vo-Dinh, P.T.2    Ribou, A.C.3    Vigo, J.4    Salmon, J.M.5
  • 47
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • 3
    • Walsh DM, Selkoe DJ (2004) Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 11(3):213-228
    • (2004) Protein Pept Lett , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 48
    • 0034237803 scopus 로고    scopus 로고
    • Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines
    • 1
    • Zolese G, Falcioni G, Bertoli E, Galeazzi R, Wozniak M, Wypych Z, Gratton E, Ambrosini A (2000) Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines. Proteins 40(1):39-48
    • (2000) Proteins , vol.40 , pp. 39-48
    • Zolese, G.1    Falcioni, G.2    Bertoli, E.3    Galeazzi, R.4    Wozniak, M.5    Wypych, Z.6    Gratton, E.7    Ambrosini, A.8


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