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Volumn 1844, Issue 3, 2014, Pages 512-519

The interrelationship between ligand binding and thermal unfolding of the folate binding protein. the role of self-association and pH

Author keywords

Differential scanning calorimetry; Dynamic light scattering; Fluorescence changes associated with irreversible thermal unfolding; Folate binding protein (soluble folate receptor); Temperature dependent self association; Thermoresistant holo protein

Indexed keywords

FOLATE BINDING PROTEIN; POLYMER;

EID: 84892730066     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.12.009     Document Type: Article
Times cited : (14)

References (35)
  • 2
    • 0025336152 scopus 로고
    • Folate binding proteins
    • G.B. Henderson Folate binding proteins Annu. Rev. Nutr. 10 1990 319 335
    • (1990) Annu. Rev. Nutr. , vol.10 , pp. 319-335
    • Henderson, G.B.1
  • 3
    • 3042810407 scopus 로고    scopus 로고
    • Factors influencing levels of folate-binding protein in bovine milk
    • DOI 10.1016/j.idairyj.2004.02.006, PII S0958694604000421
    • L. Nygren-Babol, Å. Sternesjö, and L. Björck Factors influencing levels of folate-binding protein in bovine milk Int. Dairy J. 14 2004 761 765 (Pubitemid 38871442)
    • (2004) International Dairy Journal , vol.14 , Issue.9 , pp. 761-765
    • Nygren-Babol, L.1    Sternesjo, A.2    Bjorck, L.3
  • 4
    • 84874591329 scopus 로고    scopus 로고
    • Receptor-based targeting of therapeutics
    • N.K. Mehra, V. Mishra, and N.K. Jain Receptor-based targeting of therapeutics Ther. Deliv. 4 2013 369 394
    • (2013) Ther. Deliv. , vol.4 , pp. 369-394
    • Mehra, N.K.1    Mishra, V.2    Jain, N.K.3
  • 7
    • 80855130909 scopus 로고    scopus 로고
    • The interrelationship between ligand binding and self-association of the folate binding protein. The role of detergent-tryptophan interaction
    • J. Holm, C. Schou, L.N. Babol, A.J. Lawaetz, S.W. Bruun, M.Z. Hansen, and S.I. Hansen The interrelationship between ligand binding and self-association of the folate binding protein. The role of detergent-tryptophan interaction Biochim. Biophys. Acta 1810 2011 1330 1339
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 1330-1339
    • Holm, J.1    Schou, C.2    Babol, L.N.3    Lawaetz, A.J.4    Bruun, S.W.5    Hansen, M.Z.6    Hansen, S.I.7
  • 8
    • 0035723303 scopus 로고    scopus 로고
    • Ionic charge, hydrophobicity and tryptophan fluorescence of the folate binding protein isolated from cow's milk
    • DOI 10.1023/A:1013234231960
    • J. Holm, S.I. Hansen, and M. Høier-Madsen Ionic charge, hydrophobicity and tryptophan fluorescence of the FBP isolated from cow's milk Biosci. Rep. 21 2001 305 313 (Pubitemid 34208253)
    • (2001) Bioscience Reports , vol.21 , Issue.3 , pp. 305-313
    • Holm, J.1    Hansen, S.I.2    Hoier-Madsen, M.3
  • 10
    • 33746519134 scopus 로고    scopus 로고
    • Application of near-infrared and fourier transform infrared spectroscopy in the characterization of ligand-induced conformation changes in folate binding protein purified from bovine milk: Influence of buffer type and pH
    • DOI 10.1366/000370206777887099
    • S.W. Bruun, J. Holm, S.I. Hansen, and S. Jacobsen Application of near-infrared and Fourier transform infrared spectroscopy in the characterization of ligand-induced conformation changes in folate binding protein purified from bovine milk: influence of buffer type and pH Appl. Spectrosc. 60 2006 737 746 (Pubitemid 44140218)
    • (2006) Applied Spectroscopy , vol.60 , Issue.7 , pp. 737-746
    • Bruun, S.W.1    Holm, J.2    Hansen, S.I.3    Jacobsen, S.4
  • 11
    • 75749136108 scopus 로고    scopus 로고
    • A chemometric analysis of ligand-induced changes in intrinsic fluorescence of folate binding protein indicates a link between altered conformational structure and physico-chemical characteristics
    • S.W. Bruun, J. Holm, S.I. Hansen, C.M. Andersen, and L. Nørgård A chemometric analysis of ligand-induced changes in intrinsic fluorescence of folate binding protein indicates a link between altered conformational structure and physico-chemical characteristics Appl. Spectrosc. 63 2009 1315 1322
    • (2009) Appl. Spectrosc. , vol.63 , pp. 1315-1322
    • Bruun, S.W.1    Holm, J.2    Hansen, S.I.3    Andersen, C.M.4    Nørgård, L.5
  • 12
    • 84865176362 scopus 로고    scopus 로고
    • Ligand binding induces a sharp decrease in hydrophobicity of folate binding protein assessed by 1-anilinonaphthalene-8-sulphonate which suppresses self-association of the hydrophobic apo-protein
    • J. Holm, A.J. Lawaetz, and S.I. Hansen Ligand binding induces a sharp decrease in hydrophobicity of folate binding protein assessed by 1-anilinonaphthalene-8-sulphonate which suppresses self-association of the hydrophobic apo-protein Biochem. Biophys. Res. Commun. 425 2012 19 24
    • (2012) Biochem. Biophys. Res. Commun. , vol.425 , pp. 19-24
    • Holm, J.1    Lawaetz, A.J.2    Hansen, S.I.3
  • 14
    • 0019527167 scopus 로고
    • The preparation and properties of folate-binding protein from cow's milk
    • D.N. Salter, K.J. Scott, H. Slade, and P. Andrews The preparation and properties of folate-binding protein from cow's milk Biochem. J. 193 1981 469 476
    • (1981) Biochem. J. , vol.193 , pp. 469-476
    • Salter, D.N.1    Scott, K.J.2    Slade, H.3    Andrews, P.4
  • 15
    • 0020577936 scopus 로고
    • Dependence of aggregation and ligand affinity on the concentration of the folate-binding protein from cow's milk
    • S.I. Hansen, J. Holm, J. Lyngbye, T.G. Pedersen, and I. Svendsen Dependence of aggregation and ligand affinity on concentration of folate-binding protein from cow's milk Arch. Biochem. Biophys. 226 1983 636 642 (Pubitemid 13022697)
    • (1983) Archives of Biochemistry and Biophysics , vol.226 , Issue.2 , pp. 636-642
    • Hansen, S.I.1    Holm, J.2    Lyngbye, J.3
  • 17
    • 65749120723 scopus 로고    scopus 로고
    • The effect of different folate forms on denaturation of bovine folate binding protein
    • L. Nygren-Babol, and K.L. Karonen The effect of different folate forms on denaturation of bovine folate binding protein Int. Dairy J. 19 2009 437 442
    • (2009) Int. Dairy J. , vol.19 , pp. 437-442
    • Nygren-Babol, L.1    Karonen, K.L.2
  • 18
    • 22544442178 scopus 로고    scopus 로고
    • Differential scanning calorimetry in life science: Thermodynamics, stability, molecular recognition and application in drug design
    • DOI 10.2174/0929867054546564
    • G. Bruylants, J. Wouters, and C. Michaux Differential scanning calorimetry in life science: thermodynamics, stability, molecular recognition and application in drug design Curr. Med. Chem. 12 2005 2011 2020 (Pubitemid 41015178)
    • (2005) Current Medicinal Chemistry , vol.12 , Issue.17 , pp. 2011-2020
    • Bruylants, G.1    Wouters, J.2    Michaux, C.3
  • 19
    • 33846637900 scopus 로고    scopus 로고
    • Microcalorimetry of biological macromolecules
    • DOI 10.1016/j.bpc.2006.05.004, PII S0301462206001608
    • P.L. Privalov, and A.I. Dragan Microcalorimetry of biological macromolecules Biophys. Chem. 126 2007 16 24 (Pubitemid 46186628)
    • (2007) Biophysical Chemistry , vol.126 , Issue.1-3 , pp. 16-24
    • Privalov, P.L.1    Dragan, A.I.2
  • 20
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • DOI 10.1021/bi00483a001
    • K.A. Dill Dominant forces in protein folding Biochemistry 29 1990 7133 7155 (Pubitemid 20230041)
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 21
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • R.L. Baldwin How Hofmeister ion interactions affect protein stability Biophys. J. 71 1996 2056 2063 (Pubitemid 26325984)
    • (1996) Biophysical Journal , vol.71 , Issue.4 , pp. 2056-2063
    • Baldwin, R.L.1
  • 22
    • 84866339186 scopus 로고    scopus 로고
    • Modeling the influence of salt on the hydrophobic effect and protein fold stability
    • M.S. Date, and B.N. Dominy Modeling the influence of salt on the hydrophobic effect and protein fold stability Commun. Comput. Phys. 13 2013 90 106
    • (2013) Commun. Comput. Phys. , vol.13 , pp. 90-106
    • Date, M.S.1    Dominy, B.N.2
  • 23
    • 0036303785 scopus 로고    scopus 로고
    • The effects of ionic strength on protein stability: The cold shock protein family
    • DOI 10.1016/S0022-2836(02)00259-0
    • B.N. Dominy, D. Perl, F.X. Schmid, and C.L. Brooks III The effects of ionic strength on protein stability: The cold shock protein family J. Mol. Biol. 319 2002 541 554 (Pubitemid 34729478)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.2 , pp. 541-554
    • Dominy, B.N.1    Perl, D.2    Schmid, F.X.3    Brooks III, C.L.4
  • 24
    • 84924173097 scopus 로고    scopus 로고
    • Dynamic light scattering and application to proteins in solutions
    • D. Arzensek Dynamic Light Scattering and Application to Proteins in Solutions Seminar University of Ljubljana 2010 1 18
    • (2010) Seminar University of Ljubljana , pp. 1-18
    • Arzensek, D.1
  • 25
    • 1242294476 scopus 로고    scopus 로고
    • Modulation of prion protein oligomerization, aggregation, and β-sheet conversion by 4,4′-dianilino-1,1′binaphtyl - 5,5′-sulfonate (bis-ANS)
    • Y. Cordeiro, L. Mauricio, T.R. Lima, M.P.B. Gomes, D. Foguel, and J.L. Silva Modulation of prion protein oligomerization, aggregation, and β-sheet conversion by 4,4′-dianilino-1,1′binaphtyl - 5,5′-sulfonate (bis-ANS) J. Biol. Chem. 279 2004 5346 5352
    • (2004) J. Biol. Chem. , vol.279 , pp. 5346-5352
    • Cordeiro, Y.1    Mauricio, L.2    Lima, T.R.3    Gomes, M.P.B.4    Foguel, D.5    Silva, J.L.6
  • 28
    • 0004155427 scopus 로고    scopus 로고
    • fourth ed. (printed in the United States of, America)
    • L. Stryer Biochemistry fourth ed. 1999 (printed in the United States of, America)
    • (1999) Biochemistry
    • Stryer, L.1
  • 29
    • 0028941139 scopus 로고
    • Approaches to teaching fluorescence spectroscopy
    • C.A. Royer Approaches to teaching fluorescence spectroscopy Biophys. J. 68 1995 1191 1195
    • (1995) Biophys. J. , vol.68 , pp. 1191-1195
    • Royer, C.A.1
  • 30
    • 0015988783 scopus 로고
    • Some observations on the possible nutritional significance of vitamin B12-and folate-binding proteins in milk
    • J.E. Ford Some observations on the possible nutritional significance of vitamin B12-and folate-binding proteins in milk Br. J. Nutr. 31 1974 243 257
    • (1974) Br. J. Nutr. , vol.31 , pp. 243-257
    • Ford, J.E.1
  • 31
    • 0023684517 scopus 로고
    • Folate-binding protein and the absorption of folic acid in the small intestine of the suckling rat
    • J.B. Mason, and J. Selhub Folate-binding protein and the absorption of folic acid in the small intestine of the suckling rat Am. J. Clin. Nutr. 48 1988 620 625
    • (1988) Am. J. Clin. Nutr. , vol.48 , pp. 620-625
    • Mason, J.B.1    Selhub, J.2
  • 32
    • 0035746007 scopus 로고    scopus 로고
    • Glycophosphatidylinositol-anchored proteins in Paramecium tetraurelia: Possible role in chemoresponse
    • C.A. Paquette, V. Rakochy, A. Bush, and J.L. VanHouten Glycophosphatidylinositol-anchored proteins in Paramecium tetraurelia: possible role in chemoresponse J. Exp. Biol. 204 2001 2899 2910 (Pubitemid 34861396)
    • (2001) Journal of Experimental Biology , vol.204 , Issue.16 , pp. 2899-2910
    • Paquette, C.A.1    Rakochy, V.2    Bush, A.3    Van Houten, J.L.4
  • 33
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A
    • A. Bierzynski, P.S. Kim, and R.L. Baldwin A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A Proc. Natl. Acad. Sci. U. S. A. 79 1982 2470 2474
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 2470-2474
    • Bierzynski, A.1    Kim, P.S.2    Baldwin, R.L.3
  • 35
    • 0030801644 scopus 로고    scopus 로고
    • Clustering of GPI-anchored folate receptor independent of both cross-linking and association with caveolin
    • DOI 10.1007/s002329900277
    • M. Wu, J. Fan, W. Gunning, and M. Ratnam Clustering of GPI-anchored folate receptor independent of both cross-linking and association with caveolin J. Membr. Biol. 159 1997 137 147 (Pubitemid 27421355)
    • (1997) Journal of Membrane Biology , vol.159 , Issue.2 , pp. 137-147
    • Wu, M.1    Fan, J.2    Gunning, W.3    Ratnam, M.4


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