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Volumn 4, Issue 4, 2008, Pages 317-324

The effect of molecular chaperone, Alpha-Crystallin, on the heat-induced aggregation of beta-lactoglobulin

Author keywords

Alpha crystallin; Beta lactoglobulin; Crowding agent

Indexed keywords

ALPHA-CRYSTALLIN; BETA-LACTOGLOBULIN; CROWDING AGENT; DISULPHIDE BONDS; MOLECULAR CHAPERONES; PH VALUES;

EID: 58149526282     PISSN: 15533468     EISSN: None     Source Type: Journal    
DOI: 10.3844/ajbbsp.2008.317.324     Document Type: Article
Times cited : (2)

References (34)
  • 1
    • 84916555996 scopus 로고
    • Effect of binding of retinol and palmitic acid to bovine beta-lactoglobulin on its resistance to thermal denaturation
    • Puyol, P., M.D. Perez, J.M. Peiro and M. Calvo, 1994. Effect of binding of retinol and palmitic acid to bovine beta-lactoglobulin on its resistance to thermal denaturation. J. Dairy. Sci., 77: 1494-1502. http://jds.fass.org/cgi/ content/abstract/77/6/1494.
    • (1994) J. Dairy. Sci , vol.77 , pp. 1494-1502
    • Puyol, P.1    Perez, M.D.2    Peiro, J.M.3    Calvo, M.4
  • 2
    • 0001205312 scopus 로고    scopus 로고
    • Effect of heat treatment on the conformation and aggregation of beta-lactoglobulin A, B and C
    • Manderson, G.A., M.J. Hardman and L.K. Creamer, 1998. Effect of heat treatment on the conformation and aggregation of beta-lactoglobulin A, B and C: J. Agric. Food Chem., 46: 5052-5061. http://cat.inist.fr/?aModele= afficheN&cpsidt=1656578.
    • (1998) J. Agric. Food Chem , vol.46 , pp. 5052-5061
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 3
    • 0000295322 scopus 로고    scopus 로고
    • Verheul, M., S.P. Roefs and K.G. de. Kruif, 1998. Kinetics of Heat-induced aggregation of beta-lactoglobulin: J. Agric. Food Chem., 46: 896-903. http://pubs.acs.org/cgi-bin/abstract.cgi/jafcau/1998/46/i03/abs/ jf970751t.html.
    • Verheul, M., S.P. Roefs and K.G. de. Kruif, 1998. Kinetics of Heat-induced aggregation of beta-lactoglobulin: J. Agric. Food Chem., 46: 896-903. http://pubs.acs.org/cgi-bin/abstract.cgi/jafcau/1998/46/i03/abs/ jf970751t.html.
  • 4
    • 0037423721 scopus 로고    scopus 로고
    • Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of beta-lactoglobulin
    • Croguennec, T., S. Bouhallab, D. Molle, B.T. O'Kennedy and R. Mehra, 2003. Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of beta-lactoglobulin. Biochem. Biophys. Res. Commun., 301: 465-471. http://www.ncbi.nlm.nih.gov/pubmed/12565885.
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , pp. 465-471
    • Croguennec, T.1    Bouhallab, S.2    Molle, D.3    O'Kennedy, B.T.4    Mehra, R.5
  • 5
    • 0346336103 scopus 로고    scopus 로고
    • Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin
    • Livney, Y.D., E. Verespej and D.G. Dalgleish, 2003. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin: J. Agric. Food Chem., 51: 8098-8106. http://pubs.acs.org/cgi-bin/abstract.cgi/jafcau/2003/51/i27/abs/jf034582q.html.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 8098-8106
    • Livney, Y.D.1    Verespej, E.2    Dalgleish, D.G.3
  • 6
    • 0033230053 scopus 로고    scopus 로고
    • Effect of heat treatment on the circular dichroism spectra of bovine beta-lactoglobulin A, B and C
    • Manderson, G.A., L.K. Creamer and M.J. Hardman, 1999. Effect of heat treatment on the circular dichroism spectra of bovine beta-lactoglobulin A, B and C. J. Agric. Food Chem., 47: 4557-4567. http://pubs.acs.org/cgibin/abstract. cgi/jafcau/1999/47/i11/abs/jf981291m.html.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 4557-4567
    • Manderson, G.A.1    Creamer, L.K.2    Hardman, M.J.3
  • 8
    • 4143094993 scopus 로고    scopus 로고
    • Specificity of disulfide bond formation during thermal aggregation in solutions of beta-lactoglobulin B and K-casein A
    • Livney,YD
    • Livney, Y.D. and D.G. Dalgleish, 2004. Specificity of disulfide bond formation during thermal aggregation in solutions of beta-lactoglobulin B and K-casein A. J. Agric. Food. Chem, 52: 5527-5532. http://lib.bioinfo.pl/auth: Livney,YD.
    • (2004) J. Agric. Food. Chem , vol.52 , pp. 5527-5532
    • Livney, Y.D.1    Dalgleish, D.G.2
  • 9
    • 0001266819 scopus 로고    scopus 로고
    • Molecular mass distributions of heat induced beta-lactoglobulin
    • Hoffman, M.A., G. Sala, C. Olieman and C.G. de Kruif, 1997. Molecular mass distributions of heat induced beta-lactoglobulin. J. Agric. Food Chem, 45: 2949-2957. http://www.scopus.com/scopus/record/display.url?view=basic&eid=2- s2.0-0001266819&origin=resultslist&sort=plf-f&src=s&st1= Hoffmann+M.A.&st2=&sid=KfD9vGAipXdr5cM-vcXBmVj%3a50&sot=b&sdt= b&sl=26&s=AUTHOR-NAME%28Hoffmann+M.A.%29&relpos=17
    • (1997) J. Agric. Food Chem , vol.45 , pp. 2949-2957
    • Hoffman, M.A.1    Sala, G.2    Olieman, C.3    de Kruif, C.G.4
  • 11
    • 0002284922 scopus 로고
    • Modifications of high-order structures upon heating of beta-lactoglobulin:Dependence on protein concentration
    • Iammeti, S., S. Cairoli, B. de Gregory and F. Bonomi, 1995. Modifications of high-order structures upon heating of beta-lactoglobulin:Dependence on protein concentration. J. Agric. Food Chem., 43: 53-58. http://pubs.acs.org/ cgibin/abstract.cgi/jafcau/1995/43/i01/f-pdf/f-jf00049a011 .pdf?sessid=6006l3
    • (1995) J. Agric. Food Chem , vol.43 , pp. 53-58
    • Iammeti, S.1    Cairoli, S.2    de Gregory, B.3    Bonomi, F.4
  • 12
    • 0000706426 scopus 로고    scopus 로고
    • Heat induced denaturation and aggregation of beta-lactoglobulin: Kinetics of formation of hydrophobic and disulphide-linked aggregation
    • Galani, D. and R.K.O. Apenten, 1999. Heat induced denaturation and aggregation of beta-lactoglobulin: Kinetics of formation of hydrophobic and disulphide-linked aggregation. Int. J. Food Sci. Tech., 34: 467-476. http://www3.interscience.wiley.com/journal/11909 5028/abstract
    • (1999) Int. J. Food Sci. Tech , vol.34 , pp. 467-476
    • Galani, D.1    Apenten, R.K.O.2
  • 13
    • 0028290324 scopus 로고
    • Reversible and irreversible modifications of beta-lactoglobulin upon exposure to heat
    • Cairoli, S., S. Iametti and F. Bonomi, 1994. Reversible and irreversible modifications of beta-lactoglobulin upon exposure to heat. J. Protein Chem., 13: 347-354. http://www.ncbi.nlm.nih.gov/pubmed/7945798.
    • (1994) J. Protein Chem , vol.13 , pp. 347-354
    • Cairoli, S.1    Iametti, S.2    Bonomi, F.3
  • 14
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of beta-lactoglobulin
    • Roefs, S.P.F.M. and C.G. de Kruif, 1994. A model for the denaturation and aggregation of beta-lactoglobulin: Eur. J. Biochem., 226: 883-889. http://www3.interscience.wiley.com/journal/119262936/abstract.
    • (1994) Eur. J. Biochem , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    de Kruif, C.G.2
  • 15
    • 0029034730 scopus 로고
    • Temperature dependent chaperone-like activity of alpha-crystallin
    • Doi: 10.1016/0014-5793(95)00440-K
    • Raman, B., T. Ramakrishna and M.C. Rao, 1995. Temperature dependent chaperone-like activity of alpha-crystallin: FEBS Lett., 365: 133-136. Doi: 10.1016/0014-5793(95)00440-K.
    • (1995) FEBS Lett , vol.365 , pp. 133-136
    • Raman, B.1    Ramakrishna, T.2    Rao, M.C.3
  • 16
    • 0033521012 scopus 로고    scopus 로고
    • Differential temprature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates
    • Datta, S.A. and C.M. Rao, 1999. Differential temprature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates. J. Biol.Chem., 274: 34773-34778. http://www.jbc.org/cgi/content/abstract/274/49/ 34773.
    • (1999) J. Biol.Chem , vol.274 , pp. 34773-34778
    • Datta, S.A.1    Rao, C.M.2
  • 17
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • Ingolia, T. and E. Craig, 1982. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc. Natl. Acad. Sci. USA., 79: 2360-2364. http://www.pubmedcentral.nih.gov/articlerender.fcgi? artid=346193.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2360-2364
    • Ingolia, T.1    Craig, E.2
  • 18
    • 0026483279 scopus 로고
    • Alpha-Crystallin can function as a molecular chaperone
    • Horwitz, J., 1992. Alpha-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA., 89: 10449-10453. http://www. pubmedcentral.nih.gov/articlerender.fcgi?rendertype=abstract&artid=50356.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 19
    • 0035865589 scopus 로고    scopus 로고
    • Lindner, R.A., T.M. Treweek and J.A. Carver, 2001. The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.Biochem. J., 354: 79-87. http://www.biochemj.org/bj/354/0079/bj3540079.htm.
    • Lindner, R.A., T.M. Treweek and J.A. Carver, 2001. The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.Biochem. J., 354: 79-87. http://www.biochemj.org/bj/354/0079/bj3540079.htm.
  • 20
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: A structural and kinetic spectroscopic study
    • Doi:10.1016/S0022-2836(02) 00144-4
    • Carver, J.A, R.A. Lindner, C. Lyon, D. Canet, H. Hernandez, C.M. Dobson and C. Redfield, 2002. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: A structural and kinetic spectroscopic study. J. Mol. Biol., 318: 815-827. Doi:10.1016/S0022-2836(02) 00144-4.
    • (2002) J. Mol. Biol , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 21
    • 1542467586 scopus 로고    scopus 로고
    • The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin indicates a nucleation-dependent specificity
    • Devlin, G.L., J.A. Carver and S.P. Bottomley, 2003. The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin indicates a nucleation-dependent specificity. J. Biol.Chem., 278: 48644-48650. http://www.jbc.org/cgi/content/abstract/278/49/48644.
    • (2003) J. Biol.Chem , vol.278 , pp. 48644-48650
    • Devlin, G.L.1    Carver, J.A.2    Bottomley, S.P.3
  • 22
    • 0025325591 scopus 로고
    • Rapid separation of bovine beta-crystallin subunits BetaB1, BetaB2, BetaB3, BetaA4
    • Slingsby, C. and O.A. Bateman, 1990. Rapid separation of bovine beta-crystallin subunits BetaB1, BetaB2, BetaB3, BetaA4. Exp. Eye Res., 51: 21-26. http://www.ncbi.nlm.nih.gov/pubmed/2373177.
    • (1990) Exp. Eye Res , vol.51 , pp. 21-26
    • Slingsby, C.1    Bateman, O.A.2
  • 23
    • 0034030911 scopus 로고    scopus 로고
    • Effect of pH on the thermal denaturation of whey proteins in milk
    • Doi:10.1021/jf981302b S0021-8561(98)01302-8
    • Law, A.J. and J. Leaver, 2000. Effect of pH on the thermal denaturation of whey proteins in milk. J. Agric. Food Chem., 48: 672-679. Doi:10.1021/jf981302b S0021-8561(98)01302-8.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 672-679
    • Law, A.J.1    Leaver, J.2
  • 24
    • 0032533361 scopus 로고    scopus 로고
    • Structural alterations of alpha-crystallin during its chaperone action
    • Doi:10.1046/j.1432-1327.1998.2580170.x
    • Lindner, R.A., A. Kapur, M. Mariani, S.J. Titmuss and J.A. Carver, 1998. Structural alterations of alpha-crystallin during its chaperone action. Eur. J. Biochem., 258: 170-183. Doi:10.1046/j.1432-1327.1998.2580170.x.
    • (1998) Eur. J. Biochem , vol.258 , pp. 170-183
    • Lindner, R.A.1    Kapur, A.2    Mariani, M.3    Titmuss, S.J.4    Carver, J.A.5
  • 25
    • 33845967487 scopus 로고    scopus 로고
    • The effect of dextran on subunit exchange of the molecular chaperone alphaA crystallin
    • Doi:10.1016/J.Bbapap.2006.10.002
    • Ghahghaei, A., A. Rekas., W.E. Price., G.A. Carver, 2007. The effect of dextran on subunit exchange of the molecular chaperone alphaA crystallin. Biochem. Biophys. Acta.,1774: 102-111. Doi:10.1016/J.Bbapap.2006.10.002.
    • (2007) Biochem. Biophys. Acta , vol.1774 , pp. 102-111
    • Ghahghaei, A.1    Rekas, A.2    Price, W.E.3    Carver, G.A.4
  • 26
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of beta-lactoglobulin: Role of thiol group and disulphide bonds
    • Hoffman, M.A. and P.J.J.M. van Mil, 1997. Heat-induced aggregation of beta-lactoglobulin: Role of thiol group and disulphide bonds. J. Agric. Food Chem., 45: 2942-2948. http://library.wur.nl/wda/dissertations/dis3396.pdf#page= 21.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 2942-2948
    • Hoffman, M.A.1    van Mil, P.J.J.M.2
  • 27
    • 1942441014 scopus 로고    scopus 로고
    • Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers
    • Doi:10.1110/ps.03513204
    • Croguennec, T., D. Molle, R. Mehra and S. Bouhallab, 2004. Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers. Prot. Sci., 13: 1340-1346. Doi:10.1110/ps.03513204
    • (2004) Prot. Sci , vol.13 , pp. 1340-1346
    • Croguennec, T.1    Molle, D.2    Mehra, R.3    Bouhallab, S.4
  • 28
    • 0028985708 scopus 로고
    • Thermal denaturation of beta-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05
    • Doi:10.1016/0167-4838(94)00225-6
    • Qi, X.L., S. Brownlow, C. Holt and P. Sellers, 1995. Thermal denaturation of beta-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05. Biochim. Biophys. Acta., 1248: 43-49. Doi:10.1016/0167-4838(94)00225-6.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 43-49
    • Qi, X.L.1    Brownlow, S.2    Holt, C.3    Sellers, P.4
  • 29
    • 16344383300 scopus 로고    scopus 로고
    • Casein proteins as molecular chaperones
    • Doi: 10.1021/jf048329h S00218561(04)08329-3
    • Morgan, P.E., T.M. Treweek, R.A. Lindner, W.E. Price and J.A. Carver, 2005. Casein proteins as molecular chaperones. J. Agric. Food Chem., 53: 2670-2683. Doi: 10.1021/jf048329h S00218561(04)08329-3.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 2670-2683
    • Morgan, P.E.1    Treweek, T.M.2    Lindner, R.A.3    Price, W.E.4    Carver, J.A.5
  • 30
    • 0032843334 scopus 로고    scopus 로고
    • Heat-induced aggregation of beta-lactoglobulin as a function of pH
    • Hoffman, M.A. and P.J.J. M. van Mil, 1999. Heat-induced aggregation of beta-lactoglobulin as a function of pH. J. Agr. Food. Chem. 47, 1898-1905. http://www.scopus.com/scopus/record/display.url?view=basic&eid=2-s2. 0-0000008542&origin=resultslist&sort=plf-f&src=s&st1=Hoffmann+M. A.&st2=&sid=KfD9vGAip Xdr5cM-vcXBmVj%3a50&sot=b&sdt=b&sl= 26&s=AUTHOR-NAME%28Hoffmann+M.A.%29&relpos=18
    • (1999) J. Agr. Food. Chem , vol.47 , pp. 1898-1905
    • Hoffman, M.A.1    van Mil, P.J.J.M.2
  • 31
    • 0000008540 scopus 로고    scopus 로고
    • Thermal unfolding of beta-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation
    • Prabakaran, S. and S. Damodaran, 1997. Thermal unfolding of beta-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation. J. Agric. Food Chem., 45:4303-4308. http://pubs.acs.org/cgi-bin/abstract.cgi/jafcau/1997/45/i11/abs/jf970269a.html.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 32
    • 0034089645 scopus 로고    scopus 로고
    • Involvement of disulphide bonds in bovine beta-lactoglobulin B gels set thermally at various pH
    • Otte, J., M. Zakora and K.B. Qvist, 2000. Involvement of disulphide bonds in bovine beta-lactoglobulin B gels set thermally at various pH. J. Food. Sci., 65: 384-389. http://www.scopus.com/scopus/record/display.url?view= basic&eid=2-s2.0-0034089645&origin
    • (2000) J. Food. Sci , vol.65 , pp. 384-389
    • Otte, J.1    Zakora, M.2    Qvist, K.B.3
  • 33
    • 0037598659 scopus 로고    scopus 로고
    • Verheul, M., J.S. Pedersen, S.P. Roefs and K.G. de Kruif, 1999. Association behavior of native bea-lactoglobulin.Biopolymers, 49: 11-20. http://grande.nal.usda.gov/ibids/index.php?mode2=detail&origin= ibids-references&therow=644525.
    • Verheul, M., J.S. Pedersen, S.P. Roefs and K.G. de Kruif, 1999. Association behavior of native bea-lactoglobulin.Biopolymers, 49: 11-20. http://grande.nal.usda.gov/ibids/index.php?mode2=detail&origin= ibids-references&therow=644525.
  • 34
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O.B., 1995. Molten globule and protein folding. Adv. Protein. Chem., 47: 83-229. http://cat.inist.fr/?aModele=afficheN&cpsidt=11175412.
    • (1995) Adv. Protein. Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1


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