메뉴 건너뛰기




Volumn 11, Issue 2-3, 2006, Pages 135-147

Casein micelle structure: What can be learned from milk synthesis and structural biology?

Author keywords

[No Author keywords available]

Indexed keywords

COLLOIDS; DAIRY PRODUCTS; NEUTRONS; PERTURBATION TECHNIQUES; TISSUE; X RAY SCATTERING;

EID: 33744998881     PISSN: 13590294     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cocis.2005.11.005     Document Type: Review
Times cited : (222)

References (56)
  • 2
    • 0000845298 scopus 로고
    • Physical equilibria: proteins
    • Wong N.B. (Ed), Van Nostrand, Reinhold (NY)
    • Farrell Jr. H.M. Physical equilibria: proteins. In: Wong N.B. (Ed). Fundamentals of Dairy Chemistry. 3rd edition (1988), Van Nostrand, Reinhold (NY) 461-510
    • (1988) Fundamentals of Dairy Chemistry. 3rd edition , pp. 461-510
    • Farrell Jr., H.M.1
  • 3
    • 0026668858 scopus 로고
    • Structure and stability of bovine casein micelles
    • Holt C. Structure and stability of bovine casein micelles. Adv Protein Chem 43 (1992) 63-151
    • (1992) Adv Protein Chem , vol.43 , pp. 63-151
    • Holt, C.1
  • 4
    • 4143054391 scopus 로고    scopus 로고
    • Chemistry of the caseins
    • Fox P.F., and Sweeney P.L.H. (Eds), Kluwer Academic, New York (NY)
    • Swaisgood H.E. Chemistry of the caseins. In: Fox P.F., and Sweeney P.L.H. (Eds). Advanced Dairy Chemistry-1, Proteins. 3rd edition, Part A (2003), Kluwer Academic, New York (NY) 139-201
    • (2003) Advanced Dairy Chemistry-1, Proteins. 3rd edition, Part A , pp. 139-201
    • Swaisgood, H.E.1
  • 5
    • 0000055359 scopus 로고
    • Composition of milks of various species: a review
    • Jenness R., and Sloan D.E. Composition of milks of various species: a review. Dairy Sci Abstr 32 (1970) 599-610
    • (1970) Dairy Sci Abstr , vol.32 , pp. 599-610
    • Jenness, R.1    Sloan, D.E.2
  • 7
    • 0001847418 scopus 로고
    • Caseins as calcium binding proteins
    • Thompson M.P. (Ed), CRC Press, Boca Raton (FL)
    • Farrell Jr. H.M., and Thompson M.P. Caseins as calcium binding proteins. In: Thompson M.P. (Ed). Calcium Binding Proteins vol. II (1988), CRC Press, Boca Raton (FL) 117-137
    • (1988) Calcium Binding Proteins , vol.II , pp. 117-137
    • Farrell Jr., H.M.1    Thompson, M.P.2
  • 9
    • 0542415084 scopus 로고
    • Modeling calcium-induced solubility in caprine milk systems using a thermodynamic linkage approach
    • Mora-Gutierrez A., Farrell Jr. H.M., Basch J.J., and Kumosinski T.F. Modeling calcium-induced solubility in caprine milk systems using a thermodynamic linkage approach. J Dairy Sci 76 (1993) 3689-3710
    • (1993) J Dairy Sci , vol.76 , pp. 3689-3710
    • Mora-Gutierrez, A.1    Farrell Jr., H.M.2    Basch, J.J.3    Kumosinski, T.F.4
  • 10
    • 0002429127 scopus 로고
    • Association of caseins and casein micelle structure
    • Fox P.F. (Ed), Applied Science, London, UK
    • Schmidt D.G. Association of caseins and casein micelle structure. In: Fox P.F. (Ed). Developments in Dairy Chemistry vol. 1 (1982), Applied Science, London, UK 61-86
    • (1982) Developments in Dairy Chemistry , vol.1 , pp. 61-86
    • Schmidt, D.G.1
  • 11
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Fox P.F., and Sweeney P.L.H. (Eds), Kluwer Academic, New York (NY)
    • De Kruif C.G., and Holt C. Casein micelle structure, functions and interactions. In: Fox P.F., and Sweeney P.L.H. (Eds). Advanced Dairy Chemistry-1, Proteins. 3rd edition, Part A (2003), Kluwer Academic, New York (NY) 233-276
    • (2003) Advanced Dairy Chemistry-1, Proteins. 3rd edition, Part A , pp. 233-276
    • De Kruif, C.G.1    Holt, C.2
  • 12
    • 0032520111 scopus 로고    scopus 로고
    • A core-shell model of calcium phosphate nanoclusters stabilized by β-casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron scattering measurements
    • Holt C., Timmins P.A., Errington N., and Leaver J. A core-shell model of calcium phosphate nanoclusters stabilized by β-casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron scattering measurements. Eur J Biochem 252 (1998) 73-78
    • (1998) Eur J Biochem , vol.252 , pp. 73-78
    • Holt, C.1    Timmins, P.A.2    Errington, N.3    Leaver, J.4
  • 13
    • 0037963500 scopus 로고    scopus 로고
    • Casein micelle substructure and calcium phosphate interactions studied by Sephacryl column chromatography
    • Holt C. Casein micelle substructure and calcium phosphate interactions studied by Sephacryl column chromatography. J Dairy Sci 81 (1998) 2994-3003
    • (1998) J Dairy Sci , vol.81 , pp. 2994-3003
    • Holt, C.1
  • 15
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: casting light on black boxes, the structure of dairy products
    • Horne D.S. Casein interactions: casting light on black boxes, the structure of dairy products. Int Dairy J 8 (1998) 171-177
    • (1998) Int Dairy J , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 16
    • 0032818601 scopus 로고    scopus 로고
    • Casein submicelles: do they exist?
    • This represents a critical review of the submicelle controversy
    • Walstra P. Casein submicelles: do they exist?. Int Dairy J 9 (1999) 189-192 This represents a critical review of the submicelle controversy
    • (1999) Int Dairy J , vol.9 , pp. 189-192
    • Walstra, P.1
  • 17
    • 0016152073 scopus 로고
    • Casein kinase from the Golgi apparatus of lactating mammary gland
    • Bingham E.W., and Farrell Jr. H.M. Casein kinase from the Golgi apparatus of lactating mammary gland. J Biol Chem 249 (1974) 3647-3651
    • (1974) J Biol Chem , vol.249 , pp. 3647-3651
    • Bingham, E.W.1    Farrell Jr., H.M.2
  • 19
    • 20344389812 scopus 로고    scopus 로고
    • Reconstitution of endoplasmic reticulum-associated degradation using yeast membranes and cytosol
    • Lee R.J., McCracken A.A., and Brodsky J.L. Reconstitution of endoplasmic reticulum-associated degradation using yeast membranes and cytosol. Methods Mol Biol 301 (2005) 175-184
    • (2005) Methods Mol Biol , vol.301 , pp. 175-184
    • Lee, R.J.1    McCracken, A.A.2    Brodsky, J.L.3
  • 20
    • 0036516861 scopus 로고    scopus 로고
    • Molten globule structures in milk proteins: implications for potential new structure-function relationships
    • Farrell Jr. H.M., Qi P.X., Brown E.M., Cooke P.H., Tunick M.H., Wickham E.D., et al. Molten globule structures in milk proteins: implications for potential new structure-function relationships. J Dairy Sci 85 (2002) 459-471
    • (2002) J Dairy Sci , vol.85 , pp. 459-471
    • Farrell Jr., H.M.1    Qi, P.X.2    Brown, E.M.3    Cooke, P.H.4    Tunick, M.H.5    Wickham, E.D.6
  • 22
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke R., and Lilie H. Folding and association of oligomeric and multimeric proteins. Adv Protein Chem 53 (2000) 329-401
    • (2000) Adv Protein Chem , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 23
    • 0038723712 scopus 로고    scopus 로고
    • Comparison of native and recombinant non-phosphorylated human beta-casein: further evidence for a unique beta-casein folding pattern
    • Bu H., Sood S.M., and Slattery C.W. Comparison of native and recombinant non-phosphorylated human beta-casein: further evidence for a unique beta-casein folding pattern. Arch Biochem Biophys 415 (2003) 213-220
    • (2003) Arch Biochem Biophys , vol.415 , pp. 213-220
    • Bu, H.1    Sood, S.M.2    Slattery, C.W.3
  • 25
    • 0042856750 scopus 로고    scopus 로고
    • Environmental influences on bovine κ-casein: reduction and conversion to fibrillar (amyloid) structures
    • Farrell Jr. H.M., Cooke P.H., Wickham E.D., Piotrowski E.G., and Hoagland P.D. Environmental influences on bovine κ-casein: reduction and conversion to fibrillar (amyloid) structures. J Protein Chem 24 (2002) 259-273
    • (2002) J Protein Chem , vol.24 , pp. 259-273
    • Farrell Jr., H.M.1    Cooke, P.H.2    Wickham, E.D.3    Piotrowski, E.G.4    Hoagland, P.D.5
  • 27
    • 0032703108 scopus 로고    scopus 로고
    • s1-Casein is required for the efficient transport of β- and κ-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells
    • s1-Casein is required for the efficient transport of β- and κ-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells. J Cell Sci 112 (1999) 3399-3412
    • (1999) J Cell Sci , vol.112 , pp. 3399-3412
    • Chanat, E.1    Martin, P.2    Ollivier-Bosquet, M.3
  • 30
    • 0032514615 scopus 로고    scopus 로고
    • GroEL-GroES-mediated protein folding requires an intact central cavity
    • Wang J.D., Michelitsch M.D., and Weissmann J.S. GroEL-GroES-mediated protein folding requires an intact central cavity. Proc Natl Acad Sci U S A 95 (1998) 12163-12168
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12163-12168
    • Wang, J.D.1    Michelitsch, M.D.2    Weissmann, J.S.3
  • 31
    • 0141682734 scopus 로고    scopus 로고
    • Poly-l-lysine enhances the protein disaggregation activity of ClpB
    • Strub C., Schlicker C., Buku B., and Mogk A. Poly-l-lysine enhances the protein disaggregation activity of ClpB. FEBS Lett 553 (2003) 125-130
    • (2003) FEBS Lett , vol.553 , pp. 125-130
    • Strub, C.1    Schlicker, C.2    Buku, B.3    Mogk, A.4
  • 32
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579 (2005) 3346-3354
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 34
    • 0026571308 scopus 로고
    • Distribution of ADPase activity in the lactating rat mammary gland and its possible role in an ATP cycle in the Golgi apparatus
    • Farrell Jr. H.M., Leung C.T., and Wickham E.D. Distribution of ADPase activity in the lactating rat mammary gland and its possible role in an ATP cycle in the Golgi apparatus. Arch Biochem Biophys 292 (1992) 368-375
    • (1992) Arch Biochem Biophys , vol.292 , pp. 368-375
    • Farrell Jr., H.M.1    Leung, C.T.2    Wickham, E.D.3
  • 35
    • 0021087801 scopus 로고
    • Casein kinase activity in rat mammary gland Golgi vesicles, phosphorylation of endogenous caseins
    • West D.W., and Clegg R.A. Casein kinase activity in rat mammary gland Golgi vesicles, phosphorylation of endogenous caseins. Eur J Biochem 137 (1983) 215-220
    • (1983) Eur J Biochem , vol.137 , pp. 215-220
    • West, D.W.1    Clegg, R.A.2
  • 36
    • 14644394287 scopus 로고    scopus 로고
    • A window on biomineralization
    • Veis A. A window on biomineralization. Science 307 (2005) 1419-1420
    • (2005) Science , vol.307 , pp. 1419-1420
    • Veis, A.1
  • 39
    • 0036715426 scopus 로고    scopus 로고
    • Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes
    • Thorpe C., Hoober K.L., Raje S., Glynn N.M., Burnside J., Turi G.K., et al. Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys 405 (2002) 1-12
    • (2002) Arch Biochem Biophys , vol.405 , pp. 1-12
    • Thorpe, C.1    Hoober, K.L.2    Raje, S.3    Glynn, N.M.4    Burnside, J.5    Turi, G.K.6
  • 40
    • 0016798404 scopus 로고
    • Purification of sulfhydryl oxidase from bovine milk
    • Janolino V.G., and Swaisgood H.E. Purification of sulfhydryl oxidase from bovine milk. J Biol Chem 250 (1975) 2532-2538
    • (1975) J Biol Chem , vol.250 , pp. 2532-2538
    • Janolino, V.G.1    Swaisgood, H.E.2
  • 41
    • 0011444632 scopus 로고
    • Physical properties of milk
    • Wong N.B. (Ed), Van Nostrand, Reinhold (NY)
    • Sherbon J.W. Physical properties of milk. In: Wong N.B. (Ed). Fundamentals of Dairy Chemistry. 3rd edition (1988), Van Nostrand, Reinhold (NY) 409-460
    • (1988) Fundamentals of Dairy Chemistry. 3rd edition , pp. 409-460
    • Sherbon, J.W.1
  • 42
    • 0018461571 scopus 로고
    • Post-secretory aggregation of caseins
    • Brooker B.E., and Holt C. Post-secretory aggregation of caseins. J Dairy Res 46 (1979) 193-195
    • (1979) J Dairy Res , vol.46 , pp. 193-195
    • Brooker, B.E.1    Holt, C.2
  • 43
    • 0029763127 scopus 로고    scopus 로고
    • Particle sizes of purified κ-casein: metal effect and correspondence with predicted three-dimensional molecular models
    • Farrell Jr. H.M., Kumosinski T.F., Cooke P.H., King G., Hoagland P.D., Wickham E.D., et al. Particle sizes of purified κ-casein: metal effect and correspondence with predicted three-dimensional molecular models. J Protein Chem 15 (1996) 435-1945
    • (1996) J Protein Chem , vol.15 , pp. 435-1945
    • Farrell Jr., H.M.1    Kumosinski, T.F.2    Cooke, P.H.3    King, G.4    Hoagland, P.D.5    Wickham, E.D.6
  • 44
    • 0028987236 scopus 로고
    • Lactation is disrupted by α-lactalbumin deficiency and can be restored by human α-lactalbumin gene replacement in mice
    • Stacey A., Schnicke A., Kerr M., Scott A., Mckee C., Cottingham I., et al. Lactation is disrupted by α-lactalbumin deficiency and can be restored by human α-lactalbumin gene replacement in mice. Proc Natl Acad Sci U S A 92 (1995) 2835-2839
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2835-2839
    • Stacey, A.1    Schnicke, A.2    Kerr, M.3    Scott, A.4    Mckee, C.5    Cottingham, I.6
  • 45
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • Timasheff S.N. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 41 (2002) 13473-13482
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1
  • 46
    • 84959986405 scopus 로고
    • The effects of sucrose and lactose on the sizes of casein micelles reconstituted from bovine caseins
    • Mozersky S.M., Farrell Jr. H.M., and Barford R.A. The effects of sucrose and lactose on the sizes of casein micelles reconstituted from bovine caseins. J Dairy Sci 74 (1991) 2382-2393
    • (1991) J Dairy Sci , vol.74 , pp. 2382-2393
    • Mozersky, S.M.1    Farrell Jr., H.M.2    Barford, R.A.3
  • 47
    • 0642333026 scopus 로고    scopus 로고
    • Oxygen-17 nuclear magnetic resonance studies of bovine and caprine casein hydration and activity in deuterated sugar solutions
    • Mora-Gutierrez A., Kumosinski T.F., and Farrell Jr. H.M. Oxygen-17 nuclear magnetic resonance studies of bovine and caprine casein hydration and activity in deuterated sugar solutions. J Agric Food Chem 45 (1997) 4545-4553
    • (1997) J Agric Food Chem , vol.45 , pp. 4545-4553
    • Mora-Gutierrez, A.1    Kumosinski, T.F.2    Farrell Jr., H.M.3
  • 48
    • 0030524955 scopus 로고    scopus 로고
    • Correlation of refined models for casein submicelles with electron microscopic studies of casein
    • Kumosinski T.F., Uknalis J., Cooke P.H., and Farrell Jr. H.M. Correlation of refined models for casein submicelles with electron microscopic studies of casein. Lebensm Wiss Technol 29 (1996) 326-333
    • (1996) Lebensm Wiss Technol , vol.29 , pp. 326-333
    • Kumosinski, T.F.1    Uknalis, J.2    Cooke, P.H.3    Farrell Jr., H.M.4
  • 49
    • 0347359172 scopus 로고    scopus 로고
    • Rethinking casein micelle structure using electron microscopy
    • McMahon D.J., and McManus W.R. Rethinking casein micelle structure using electron microscopy. J Dairy Sci 81 (1998) 2985-2993
    • (1998) J Dairy Sci , vol.81 , pp. 2985-2993
    • McMahon, D.J.1    McManus, W.R.2
  • 51
    • 0018459402 scopus 로고
    • The role of calcium phosphate and citrate ions in the stabilization of casein micelles
    • Visser J., Schaier R.W., and van Gokkom M. The role of calcium phosphate and citrate ions in the stabilization of casein micelles. J Dairy Res 46 (1979) 333-335
    • (1979) J Dairy Res , vol.46 , pp. 333-335
    • Visser, J.1    Schaier, R.W.2    van Gokkom, M.3
  • 52
    • 0014936059 scopus 로고
    • Micelle forming characteristics of monomeric and covalent polymeric kappa-caseins
    • Talbot B., and Waugh D.F. Micelle forming characteristics of monomeric and covalent polymeric kappa-caseins. Biochemistry (1970) 2807-2813
    • (1970) Biochemistry , pp. 2807-2813
    • Talbot, B.1    Waugh, D.F.2
  • 53
    • 0023733240 scopus 로고
    • Determination of the quaternary structural states of bovine casein by small-angle X-ray scattering: submicellar and micellar forms
    • Kumosinski T.F., Pessen H., Farrell Jr. H.M., and Brumberger H. Determination of the quaternary structural states of bovine casein by small-angle X-ray scattering: submicellar and micellar forms. Arch Biochem Biophys 266 (1988) 548-561
    • (1988) Arch Biochem Biophys , vol.266 , pp. 548-561
    • Kumosinski, T.F.1    Pessen, H.2    Farrell Jr., H.M.3    Brumberger, H.4
  • 54
    • 0020483891 scopus 로고
    • Small-angle neutron scattering study of bovine casein micelles and submicelles
    • Stothart P.H., and Cebula D.J. Small-angle neutron scattering study of bovine casein micelles and submicelles. J Mol Biol 160 (1982) 391-395
    • (1982) J Mol Biol , vol.160 , pp. 391-395
    • Stothart, P.H.1    Cebula, D.J.2
  • 56
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11 (2002) 739-756
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.