메뉴 건너뛰기




Volumn 90, Issue 1, 2007, Pages 75-89

Evidence for fibril-like structure in bovine casein micelles

Author keywords

Casein micelle; Congo red; Protofibril; Thioflavin T

Indexed keywords

BOVINAE;

EID: 35748971792     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(07)72610-3     Document Type: Article
Times cited : (36)

References (39)
  • 2
    • 0023803129 scopus 로고
    • Controlled environment vitrification system: An improved sample preparation technique
    • Bellare, J. R., H. T. Davis, L. E. Scriven, and Y. Talmon. 1988. Controlled environment vitrification system: An improved sample preparation technique. J. Electron Microsc. Tech. 10:87-111.
    • (1988) J. Electron Microsc. Tech , vol.10 , pp. 87-111
    • Bellare, J.R.1    Davis, H.T.2    Scriven, L.E.3    Talmon, Y.4
  • 4
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron x-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous /3-sheet helix
    • Blake, C., and L. Serpell. 1996. Synchrotron x-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous /3-sheet helix. Structure 4:989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 5
    • 0014814906 scopus 로고
    • Examination of the mineral composition of the micelle of milk by gel filtration
    • Boulet, M., A. Yang, and R. R. Riel. 1970. Examination of the mineral composition of the micelle of milk by gel filtration. Can. J. Biochem. 48:816-822.
    • (1970) Can. J. Biochem , vol.48 , pp. 816-822
    • Boulet, M.1    Yang, A.2    Riel, R.R.3
  • 6
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation
    • Carrotta, R., R. Bauer, R. Waninge and C. Rischel. 2001. Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation. Protein Sci. 10:1312-1318.
    • (2001) Protein Sci , vol.10 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 7
    • 85031452313 scopus 로고    scopus 로고
    • de Kruif, C. G., and C. Holt. 2003. Casein micelle structure, functions and interactions. Pages 233-276 in Advanced Dairy Chemistry, 1: Proteins. 3rd ed. P. F. Fox and P. L. H. McSweeney, ed. Kluwer, New York, NY.
    • de Kruif, C. G., and C. Holt. 2003. Casein micelle structure, functions and interactions. Pages 233-276 in Advanced Dairy Chemistry, Volume 1: Proteins. 3rd ed. P. F. Fox and P. L. H. McSweeney, ed. Kluwer, New York, NY.
  • 8
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. 2003. Protein folding and misfolding. Nature 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 10
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study
    • Dzwolak, W., and M. Pecul. 2005. Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study. FEBS Lett. 579:6601-6603.
    • (2005) FEBS Lett , vol.579 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 11
    • 0000845298 scopus 로고
    • Physical equilibria: Proteins
    • 3rd ed. N. Wong, ed. Van Nostrand, New York, NY
    • Farrell, H. M., Jr. 1988. Physical equilibria: Proteins. Pages 461-510 in Fundamentals of Dairy Chemistry. 3rd ed. N. Wong, ed. Van Nostrand, New York, NY.
    • (1988) Fundamentals of Dairy Chemistry , pp. 461-510
    • Farrell Jr., H.M.1
  • 12
    • 0042856750 scopus 로고    scopus 로고
    • Environmental influences on bovine κ-casein: Reduction and conversion to fibrillar (amyloid) structures
    • Farrell, H. M., Jr., P. H. Cooke, E. D. Wickham, E. G. Piotrowski, and P. D. Hoagland. 2003. Environmental influences on bovine κ-casein: Reduction and conversion to fibrillar (amyloid) structures. J. Protein Chem. 22:259-273.
    • (2003) J. Protein Chem , vol.22 , pp. 259-273
    • Farrell Jr., H.M.1    Cooke, P.H.2    Wickham, E.D.3    Piotrowski, E.G.4    Hoagland, P.D.5
  • 13
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloids
    • Fink, A. L. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloids. Fold. Des. 3:R9-R23.
    • (1998) Fold. Des , vol.3
    • Fink, A.L.1
  • 16
    • 0003339397 scopus 로고
    • Structure formation in acid milk gels
    • Heertje, I., J. Visser, and P. Smits. 1985. Structure formation in acid milk gels. Food Microstruct. 4:267-277.
    • (1985) Food Microstruct , vol.4 , pp. 267-277
    • Heertje, I.1    Visser, J.2    Smits, P.3
  • 17
    • 0026668858 scopus 로고
    • Structure and stability of bovine casein micelles
    • Holt, C. 1992. Structure and stability of bovine casein micelles. Adv. Protein Chem. 43:63-151.
    • (1992) Adv. Protein Chem , vol.43 , pp. 63-151
    • Holt, C.1
  • 18
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins: Interpretation of the primary and secondary structures of the αs1-, β- and κ-caseins
    • Holt, C., and L. Sawyer. 1993. Caseins as rheomorphic proteins: Interpretation of the primary and secondary structures of the αs1-, β- and κ-caseins. J. Chem. Soc. Faraday Trans. 89:2683-2692.
    • (1993) J. Chem. Soc. Faraday Trans , vol.89 , pp. 2683-2692
    • Holt, C.1    Sawyer, L.2
  • 19
    • 0000547124 scopus 로고
    • Preparation and properties of a salt solution which simulates milk ultrafiltrate
    • Jenness, R., and J. Koops. 1962. Preparation and properties of a salt solution which simulates milk ultrafiltrate. Neth. Milk Dairy J. 16:153-164.
    • (1962) Neth. Milk Dairy J , vol.16 , pp. 153-164
    • Jenness, R.1    Koops, J.2
  • 21
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behaviour
    • Kelly, J. W. 1996. Alternative conformations of amyloidogenic proteins govern their behaviour. Curr. Opin. Struct. Biol. 6:11-17.
    • (1996) Curr. Opin. Struct. Biol , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 23
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk, W. E., R. F. Jacob, and R. P. Mason. 1999. Quantifying amyloid by Congo red spectral shift assay. Meth. Enzymol. 309:285-305.
    • (1999) Meth. Enzymol , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 24
    • 0024363054 scopus 로고
    • Two simple methods for quantifying low-affinity dye-substrate binding
    • Klunk, W. E., J. W. Pettegrew, and D. J. Abraham. 1989. Two simple methods for quantifying low-affinity dye-substrate binding. J. Histochem. Cytochem. 37:1293-1297.
    • (1989) J. Histochem. Cytochem , vol.37 , pp. 1293-1297
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 25
    • 0027661562 scopus 로고
    • Three dimensional molecular modeling of bovine caseins: A refined energy-minimized κ-casein structure
    • Kumosinki, T. F., E. M. Brown, and H. M. Farrell, Jr. 1993. Three dimensional molecular modeling of bovine caseins: A refined energy-minimized κ-casein structure. J. Dairy Sci. 76:2507-2520.
    • (1993) J. Dairy Sci , vol.76 , pp. 2507-2520
    • Kumosinki, T.F.1    Brown, E.M.2    Farrell Jr., H.M.3
  • 26
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin-T
    • LeVine, H., III. 1999. Quantification of β-sheet amyloid fibril structures with thioflavin-T. Meth. Enzymol. 309:274-284.
    • (1999) Meth. Enzymol , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 27
    • 0001737480 scopus 로고    scopus 로고
    • Fluorescent heterogeneities in turbid media: Limits of detection, characterization and comparison with absorption
    • Li, X., B. Chance, and A. G. Yodh. 1998. Fluorescent heterogeneities in turbid media: Limits of detection, characterization and comparison with absorption. Appl. Opt. 37:6833-6844.
    • (1998) Appl. Opt , vol.37 , pp. 6833-6844
    • Li, X.1    Chance, B.2    Yodh, A.G.3
  • 28
    • 0347359172 scopus 로고    scopus 로고
    • Rethinking casein micelle structure using electron microscopy
    • McMahon, D. J., and W. R. McManus. 1998. Rethinking casein micelle structure using electron microscopy. J. Dairy Sci. 81:2985-2993.
    • (1998) J. Dairy Sci , vol.81 , pp. 2985-2993
    • McMahon, D.J.1    McManus, W.R.2
  • 29
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models for amyloid fibril structure
    • Nelson, R., and D. Eisenberg. 2006. Recent atomic models for amyloid fibril structure. Curr. Opin. Struct. Biol. 16:260-265.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 30
    • 0345436424 scopus 로고
    • Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry
    • Paulsson, M., and P. Dejmek. 1990. Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry. J. Dairy Sci. 73:590-600.
    • (1990) J. Dairy Sci , vol.73 , pp. 590-600
    • Paulsson, M.1    Dejmek, P.2
  • 31
    • 84975573782 scopus 로고
    • Influence of scattering on fluorescence spectra of dilute solutions obtained with the Aminco-Bowman spectrophotofluorometer
    • Price, J. M., M. Kailhara, and H. R. Howerton. 1962. Influence of scattering on fluorescence spectra of dilute solutions obtained with the Aminco-Bowman spectrophotofluorometer. Appl. Opt. 1:521-533.
    • (1962) Appl. Opt , vol.1 , pp. 521-533
    • Price, J.M.1    Kailhara, M.2    Howerton, H.R.3
  • 33
    • 85031437398 scopus 로고    scopus 로고
    • Rollema, H. S. 1992. Casein association and micelle formation. Pages 111-140 in Advanced Dairy Chemistry 1: Proteins. 2nd ed. P. F. Fox ed. Elvsevier, Barking, UK.
    • Rollema, H. S. 1992. Casein association and micelle formation. Pages 111-140 in Advanced Dairy Chemistry Volume 1: Proteins. 2nd ed. P. F. Fox ed. Elvsevier, Barking, UK.
  • 34
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and x-ray diffraction
    • Sunde, M., and C. Blake. 1997. The structure of amyloid fibrils by electron microscopy and x-ray diffraction. Adv. Protein Chem. 50:123-159.
    • (1997) Adv. Protein Chem , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 35
    • 85031435298 scopus 로고    scopus 로고
    • Swaisgood, H. E. 2003. Chemistry of caseins. Pages 139-202 in Advanced Dairy Chemistry 1: Proteins. 3rd ed. P. F. Fox and P. L. H. McSweeney, ed. Kluwer, New York, NY.
    • Swaisgood, H. E. 2003. Chemistry of caseins. Pages 139-202 in Advanced Dairy Chemistry Volume 1: Proteins. 3rd ed. P. F. Fox and P. L. H. McSweeney, ed. Kluwer, New York, NY.
  • 36
    • 0012189549 scopus 로고
    • Physical parameters of κ-casein from cow's milk
    • Swaisgood, H. E., J. R. Brunner, and H. A. Lillevik. 1964. Physical parameters of κ-casein from cow's milk. Biochemistry 3: 1616-1623.
    • (1964) Biochemistry , vol.3 , pp. 1616-1623
    • Swaisgood, H.E.1    Brunner, J.R.2    Lillevik, H.A.3
  • 37
    • 0001677248 scopus 로고
    • Staining and drying-induced artefacts in electron microscopy of surfactant dispersions
    • Talmon, Y. 1983. Staining and drying-induced artefacts in electron microscopy of surfactant dispersions. J. Colloid Interf. Sci. 93:366-382.
    • (1983) J. Colloid Interf. Sci , vol.93 , pp. 366-382
    • Talmon, Y.1
  • 38
    • 29344455729 scopus 로고    scopus 로고
    • Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones αS- and β-casein
    • Thorn, D. C., S. Meechan, M. Sunde, A. Rekas, S. L. Gras, C. E. McPhee, C. M. Dobson, M. R. Wilson, and J. A. Carver. 2005. Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones αS- and β-casein. Biochemistry 44:17027-17036.
    • (2005) Biochemistry , vol.44 , pp. 17027-17036
    • Thorn, D.C.1    Meechan, S.2    Sunde, M.3    Rekas, A.4    Gras, S.L.5    McPhee, C.E.6    Dobson, C.M.7    Wilson, M.R.8    Carver, J.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.