Chemistry of the caseins

Advanced Dairy Chemistry: Volume 1A: Proteins: Basic Aspects, 4th Edition

Volumn , Issue , 2013, Pages 135-160

  Huppertz, T ^a  

^a NIZO FOOD RESEARCH   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; DAIRIES; GENES; MICELLES; PROTEINS; SULFUR COMPOUNDS;

AMINO ACID SEQUENCE; BUILDING BLOCKES; CASEIN MICELLES; GENETIC VARIATION; HIGHER-ORDER STRUCTURE; POST-TRANSLATIONAL MODIFICATIONS; SECONDARY AND TERTIARY STRUCTURES; SELF-ASSOCIATIONS;

CASEIN;

EID: 84948965727     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-4714-6_4     Document Type: Chapter

References (164)

1. Adzhubei, A.A. and Sternberg, M.J.E. (1993). Lefthanded polyproline II helices commonly occur in globular proteins. J. Mol. Biol. 229, 472-493.
2. Andrews, A.L., Atkinson, D., Evans, M.T.A., Finer, E.G., Green, J.P., Phillips, M.C. and Robertson, R.N. (1979). The conformation and aggregation of bovine b-casein A. I. Molecular aspects of thermal aggregation. Biopolymers 18, 1105-1121.
3. Aoki, T., Toyooka, K. and Kako, Y. (1985). Role of phosphate groups in the calcium sensitivity of as2-casein. J. Dairy Sci. 68, 1624-1629.
4. Arima, S., Niki, R. and Takase, K. (1979). Structure of b-casein. J. Dairy Res. 46, 281-282.
5. Azuma, N., Nara, K. and Kanno, C. (1991). Enzymic modification of as1-casein with peptidylarginine deimi-nase: preparation of less acid-coagulable and less calcium-sensitive casein. J. Dairy Res. 58, 421-429.
6. Baumy, J.J. and Brule, G. (1988). Effect of pH and ionic strength on the binding of bivalent cations to b-casein. Lait 68, 409-418.
7. Bech, A.M. and Kristiansen, K.R. (1990). Milk protein polymorphism in Danish dairy cattle and the influence of genetic variants on milk yield. J. Dairy Res. 57, 53-62.
8. Berry, G.P. and Creamer, L.K. (1975). The association of bovine b-casein. The importance of the C-terminal region. Biochem. 14, 3542-3545.
9. Bingham, E.W., Farrell, H.M., and Carroll, R.J., Jr. (1972). Properties of dephosphorylated as1-casein. Precipitation by calcium ions and micelle formation. Biochem. 11, 2450-2454.
10. Bonsing, J., Ring, J.M., Stewart, A.F. and MacKinlay, A.G. (1988). Complete nucleotide sequence of the bovine beta-casein gene. Aust. J. Biol. Sci. 41, 527-537
11. Bouniol, C., Printz, C. and Mercier J.-C. (1993). Bovine aS2-casein D is generated by exon VIII skipping. Gene 128, 289-293.
12. Brignon, G., Ribadeau-Dumas, B. and Mercier, J.-C. (1976). Premiers elements de structure primaire des caseines a _ bovines. FEBS Lett. 71,111-116.
13. Brignon, G.B., Ribadeau-Dumas, B., Mercier, J.-C., Pelissier, J.-P. and Das, B.C. (1977). The complete amino acid sequence of bovine aS2-casein. FEBS Lett. 76, 274-279.
14. Buchheim, W. and Schmidt, D.G. (1979). On the size of monomers and polymers of b-casein. J. Dairy Res. 46, 277-280.
15. Byler, D.M. and Susi, H. (1986). Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers 25, 469-487.
16. Byler, D.M., Farrell, H.M., Jr. and Susi, H. (1988). Raman spectroscopic study of casein structure. J. Dairy Sci. 71, 2622-2629.
17. Caessens, P.W.J.R., De Jongh, H.H.J., Noide, W. and Gruppen, H. (1999). The absorption-induced secondary structure of b-casein and of distinct parts of its sequence. Biochim. Biophys. Acta 1430, 73-83.
18. Carles, C., Huet, J.-C. and Ribadeau-Dumas, B. (1988). A new strategy for primary structure determination of proteins: application to b-casein. FEBS Lett. 229, 265-272.
19. Chung, E.R., Han, S.K. and Rhim, T.J. (1995). Milk protein polymorphisms as genetic markers in Korean native cattle. Asian Austral. J. Anim. Sci. 8, 187-194.
20. Coolbear, K.P., Elgar, D.F. and Ayers, J.S. (1996). Profiling of genetic variants of bovine K-casein macropeptide by electrophoretic and chromatographic techniques. Int. Dairy J. 6, 1055-1068.
21. Corradini, C. (1969). Distribution of the genetic variants a-, b-, and K-caseins in milk from Jersey cows in The Netherlands. Neth. Milk Dairy J. 23, 79-82.
22. Creamer, L.K., Richardson, T. and Parry, D.A.D. (1981). Secondary structure of bovine a-and b-casein in solution. Arch. Biochem. Biophys. 211, 689-696.
23. Creamer, L.K., Plowman, J.E., Liddell, M.J., Smith, M.H. and Hill. J.P. (1998). Micelle stability: K-casein structure and function. J. Dairy Sci. 81, 3004-3012.
24. Dalgleish, D.G. and Parker, T.G. (1980). Binding of calcium ions to bovine as1-casein and precipitability of the protein-calcium ion complexes. J. Dairy Res. 47, 113-122.
25. Dalgleish, D.G., Paterson, E. and Horne, D.S. (1981). Kinetics of aggregation of as1-casein/Ca2+ mixtures: charge and temperature effects. Biophys. Chem. 13, 307-314.
26. Darewicz, M., Dziuba, J., Mioduszewska, H. and Minkiewicz, P. (1999). Modulation of physico-chemical properties of bovine b-casein by non-enzymatic gly-cation associated with enzymatic dephosphorylation. Acta Aliment. 28, 339-354.
27. De Kruif, C.G. and Grinberg, V.Y. (2002). Micellisation of b-casein. Colloid. Surface. A 210, 183-190.
28. De Kruif, C.G. and Holt, C. (2003). Casein micelle structure, functions and interactions, in Advanced Dairy Chemistry 1: Proteins, 3rd edn. P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic/Plenum Publishers, New York. pp 233-276.
29. De Kruif, C.G. and May, R.P. (1991). K-Casein micelles: structure, interaction and gelling studied by small-angle neutron scattering. Eur. J. Biochem. 200, 431-436.
30. De Kruif, C.G., Tuinier, R., Holt, C., Timmins, P.A. and Rollema, H.S. (2002). Physicochemical study of k-and b-casein dispersion and the effect of cross-linking by transglutaminase. Langmuir 18, 4885-4891.
31. Dong, C. and Ng-Kwai-Hang, K.F. (1998). Characterization of a nonelectrophoretic genetic variant of b-casein by peptide mapping and mass spectroscopic analysis. Int. Dairy J. 8, 967-972.
32. Dosaka, S., Kimura, T., Taneya, S., Sone, T., Kaminogawa, S. and Yamauchi, K. (1980). Polymerization of a-casein by calcium ions. Agric. Biol. Chem. 44, 2443-2448.
33. Ecroyd, H., Koudelka, T., Thorn, D.C., Williams, D.M., Devlin, G., Hoffman, P. and Carver, J.A. (2008). Dissociation from the oligomeric state is the rate-limiting step in fibril formation by K-casein. J. Biol. Chem. 283, 9012-9022.
34. Ecroyd, H., Thorn, D.C., Lui, Y. and Carver, J.A. (2010). The dissociated form of K-casein is the precursor to its amyloid fibril formation. Biochem. J. 429, 251-260.
35. Eigel, W.N., Butler, J.E., Ernstrom, C.A., Farrell, H.M., Jr., Harwalkar, V.R., Jenness, R. and Whitney, R.M. (1984). Nomenclature of proteins of cow’s milk: fifth revision. J. Dairy Sci. 67, 1599-1631.
36. Erhardt, G. (1993). A new as1-casein allele in bovine milk and its occurrence in different breeds. Anim. Genet. 24, 65-66.
37. Erhardt, G. (1996). Detection of a new K-casein variant in the milk of Pinzgauer cattle. Anim. Genet. 27, 105-107.
38. Evans, M.T.A. and Phillips, M.C. (1979). The conformation and aggregation of bovine beta-casein A. II. Thermodynamics of thermal association and the effects of changes in polar and apolar interactions on micellization. Biopolymers 18, 1123-1140.
39. Farrell, H.M. Jr., Kumosinski, T.F., Thompson, M.P. and Pulaski, P. (1988). Calcium induced associations of the caseins: a thermodynamic linkage approach to precipitation and resolubilization. Arch. Biochem. Biophys. 265, 146-158.
40. Farrell, H.M. Jr., Kumosinski, T.F., Cooke, P.H., King, G., Hoagland, P.D., Wickham, E.D., Dower, H.J. and Groves, M.L. (1996). Particle size of purified K-casein: metal effect and correspondence with predicted threedimensional molecular models. J. Prot. Chem. 15, 435-445.
41. Farrell, H.M. Jr., Wickham, E.D., Unruh, J.J., Qi, P.X. and Hoagland, P.D. (2001). Secondary structure studies of bovine caseins: temperature dependence of b-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloid 15, 341-354.
42. Farrell, H.M. Jr., Cooke, P.H., Wickham, E.D., Piotrowski, E.G. and Hoagland, P.D. (2003). Environmental influences of bovine K-casein: reduction and conversion to fibrillar (amyloid) structures. J. Prot. Chem. 22, 259-273.
43. Farrell, H.M., Jr., Jimenez-Flores, R., Bleck, G.T., Brown, E.M., Butler, J.E., Creamer, L.K., Hicks, C.L., Hollar, C.M., Ng-Kwai-Hang, K.F. and Swaisgood, H.E. (2004). Nomenclature of the proteins of cows’ milk: sixth revision. J. Dairy Sci. 87, 1641-1674.
44. Farrell, H.M. Jr., Malin, E.L., Brown, E.M. and Mora-Gutierrez, A. (2009). Review of the chemistry of as2-casein and the generation of a homolgous molecular model to explain its properties. J. Dairy Sci. 92, 1338-1353.
45. Gagnard, S., Zuev, Y., Gaudin, J.-C., Fedotov, V., Choiset, Y., Axelos, M.A.V., Chobert, J.-M. and Haertle, T. (2007). Modifications of the charges at the N-terminus of bovine b-casein: consequences on its structure and its micellisation. Food Hydrocolloid 21, 180-190.
46. Garnier, J. (1966). Conformation of b-casein in solution. Analysis of a thermal transition between 5 and 40°C. J. Mol. Biol. 19, 586-590.
47. Garnier, J., Osguthorpe, D.J. and Robinson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120.
48. Gouldsworthy, A.M., Leaver, J. and Banks, J.M. (1996). Application of a mass spectrometry sequencing technique for identifying peptides present in Cheddar cheese. Int. Dairy J. 6, 781-791.
49. Graham, E.R.B., Malcolm, G.N. and McKenzie, H.A. (1984). On the isolation and conformation of bovine b-casein A1. Int. J. Biol. Macromol. 6, 155-161.
50. Griffin, M.C.A., Price, J.C. and Martin, S.R. (1986). Effect of alcohols on the structure of caseins: circular dichroism studies of κ-casein A. Int. J. Biol. Macromol.8,367-371.
51. Groenen, M.A.M., Dijkhof, R.E.M., Verstege, A.J.M. and Van der Poel, J.J. (1993). The complete sequence of the gene encoding bovine aS2-casein. Gene 123, 187-193.
52. Grosclaude, F. (1988). Le polymorphisme genetique des principales actoproteines bovines. Relations avec la quantite, la composition et les aptitudes fromageres du lait. INRA Prod. Anim. 1, 5-17.
53. Grosclaude, F., Mercier, J.-C. and Ribadeau-Dumas, B. (1969). Sur la localisation, dans la séquence COOH-terminale de la caseine alpha-S1 bovine, de la substitution GLU-GLY différenciant les variants génétiques B et C. CR Acad. Sci. D: Sci. Natur. 268, 3133-3136.
54. Grosclaude, F., Mahe, M.-F., Mercier, J.-C. and Ribadeua-Dumas, B. (1970). Localisation, dans la partie NH2-terminale de la caséine a, bovine, d’une délétion de 13 acides aminés différenciant le variant a des variants B et C. FEBS Lett. 11, 109-112.
55. Grosclaude, F., Mahe, M.-F., Mercier, J.-C. and Ribadeau-Dumas, B. (1972). Caracterisation des variants genet-iques des caseines as1 et b bovines. Eur. J. Biochem.26, 328-337.
56. Grosclaude, F., Mahe, M.-F. and Ribadeau-Dumas, B. (1973). Structure primaire de la caseine as1-et de la caseine b-bovine. Eur. J. Biochem. 40, 323-324.
57. Grosclaude, F., Mahe, M.-F. and Mercier, J.-C. (1974a). Comparison du polymorphisme genetique des lacto-proteines du zebu et des bovines. Ann. Genet. Sel. Anim. 6, 305-329.
58. Grosclaude, F., Mahe, M.-F. and Voglino, G.-F. (1974b). Le variant bE et le code de phosphorylation des caseins bovines. FEBS Lett. 45, 3-5.
59. Grosclaude, F., Mahe, M.-F., Mercier, J.-C., Bonnemaire, J. and Teissier, J.H. (1976). Polymorphisme des lactoproteines de bovines Nepalais. Polymorphisme des caseine a-mineurs. Ann. Genet. Sel. Evol. 8, 461-479.
60. Grosclaude F., Joudrier, P. and Mahe, M.-F. (1978). Polymorphisme de la caseine aS2 bovine: Etroite liaison du locus aS2-Cn avec les loci as1-Cn, b-Cn et K-Cn; mise en evidence d’une deletion dans le variant aS2-Cn D. Ann. Genet. Sel. Anim. 10, 313-327.
61. Grosclaude, F., Mahe, M.-F. and Accolas, J.P. (1982). Note sur le polymorphisme genetique des lactoproteines de bovins et de yaks Mongols. Ann. Genet. Sel. Anim. 14, 545-550.
62. Groves, M.L. (1969). Some minor components of casein and other phosphoproteins in milk. A review. J. Dairy Sci. 52, 1155-1165.
63. Groves, M.L., Dower, H.J. and Farrell, H.M. Jr. (1992). Reexamination of the polymeric distributions of K-casein isolated from bovine milk. J. Prot. Chem. 11, 21-27.
64. Groves, M.L., Wickham, E.D. and Farrell, H.M. Jr. (1998). Environmental effects on disulphide bonding patterns of bovine K-casein. J. Prot. Chem. 17, 73-84.
65. Han, S.K., Shin, Y.C. and Byun, H.D. (2000). Biochemical, molecular and physiological characterization of a new b-casein variant detected in Korean cattle. Anim. Genet. 31, 49-51.
66. Herskovits, T.T. (1966). On the conformation of casein. ORD properties. Biochem. 5, 1018-1026.
67. Ho, C. and Waugh, D.F. (1965). Interactions of bovine as-casein with small ions. J. Am. Chem. Soc. 87, 110-117.
68. Hoagland, P.D., Unruh, J.J., Wickham, E.D. and Farrell, M. Jr. (2001). Secondary structure of bovine as2-casein: theoretical and experimental approaches. J. Dairy Sci. 84, 1944-1949.
69. Holland, J.W., Deeth, H.C. and Alewood, P.F. (2004). Proteomic analysis of K-casein microheterogeniety. Proteomics 4, 743-752.
70. Holland, J.W., Deeth, H.C. and Alewood, P.F. (2005). Analysis of O-glycosylation site occupancy in bovine K-casein glycoforms separated by two-dimensional gel electrophoresis. Proteomics 5, 990-1002.
71. Holland, J.W., Deeth, H.C. and Alewood, P.F. (2006). Resolution and characterization of multiple isoforms of bovine K-casein by 2-DE followed by reversible cysteine-tagging enrichment strategy. Proteomics 6, 3087-3095.
72. Holt, C. and Sawyer, L. (1988). Primary and predicted secondary structures of the caseins in relation to their biological functions. Protein Eng. 2, 251-259.
73. Holt, C., Parker, T.G. and Dalgleish, D.G. (1975). The thermochemistry of reactions between as1-casein and calcium chloride. Biochim. Biophys. Acta 379, 638-644.
74. Jann, O., Ceriotti, G., Caroli, A. and Erhardt, G. (2002). A new variant in exon VII of the bovine b-casein gene (CSN2) and its distribution among European cattle breeds. J. Anim. Breed. Genet. 119, 65-68.
75. Jenness, R., Larson, B.L., McMeekin, T.L., Swanson, A.M., Whitnah, C.H. and Whitney, R.M. (1956). Nomenclature of the proteins of bovine milk. J. Dairy Sci. 39, 536-541.
76. Jimenez-Flores, R., Kang, Y.C. and Richardson, T. (1987). Cloning and sequence analysis of bovine b-casein cDNA. Biochem. Biophys. Res. Comm. 142, 617-621.
77. Kajiwara, K., Niki, R., Urakawa, H., Hiragi, Y., Donkai, N. and Nagura, M. (1988). Micellar structure of b-casein observed by small-angle X-ray scattering. Biochim. Biophys. Acta 955, 128-134.
78. Kumosinski, T.F., Brown, E.M. and Farrell, H.M. Jr. (1991). Three-dimensional molecular modeling of bovine caseins: K-casein. J. Dairy Sci. 74, 2879-2887.
79. Kumosinski, T.F., Brown, E.M. and Farrell, H.M. Jr. (1993). Refined molecular modeling of bovine caseins: a refined energy-minimized K-casein structure. J. Dairy Sci. 76, 2507-2520.
80. Leclerc, E. and Calmettes, P. (1997a). Interactions in micellar solutions of b-casein. Physica B 234-236, 207-209.
81. Leclerc, E. and Calmettes, P. (1997b). Interactions in micellar solutions of b-casein. Phys. Rev. Lett. 78, 150-153.
82. Leclerc, E. and Calmettes, P. (1998). Structure of b-casein micelles. Physica B 241-243, 1141-1143.
83. Leonil, J., Henry, G., Jouanneau, D., Delage, M.-M., Forge, V. and Putaux, J.-L. (2008). Kinetics of fibril formation of bovine K-casein indicate a conformational reaarangement as a critical step in the process. J. Mol. Biol. 381, 1267-1280.
84. Mahe, M.-F. and Grosclaude, F. (1982). Polymorphisme de la caseine aS2 des bovines: characterization du variant C du yak (Bos grunniens). Ann. Genet. Sel. Anim. 14, 401-416.
85. Mahe, M.-F., Miranda, G., Queral, R., Bado, A., Souvenir-Zafidrajaona, P. and Grosclaude, F. (1999). Genetic polymorphism of milk proteins in African Bos taurus and Bos indicus populations characterization of variants aS1-Cn H and K-Cn. J. Genet. Sel. Evol. 31, 239-253.
86. Malin, E.L., Brown, E.M., Wickham, E.D. and Farrell, H.M. Jr. (2005). Contributions of terminal peptides to associative behavior of as1-casein. J. Dairy Sci. 88, 2318-2328.
87. Manson, W., Carolan, T. and Annan, W.D. (1977). Bovine as0-casein; a phosphorylated homologue of as1-casein. Eur. J. Biochem. 78, 411-417.
88. Mariani, P. and Russo, V. (1975). Varianti genetiche delle a protein del latte nella razza. Rendena. Riv. Zootec. Vet. 3, 345-348.
89. Mariani, P., Summer, A., Anghinetti, A., Senese, C., Di Gregorio, P., Rando, P. and Serventi, P. (1995). Effects of the as1-CN G allele on the percentage distribution of caseins a,-, a-, ß-, and k-in Italian Brown cows. Ind. Latte 31, 3-13.
90. Mercier, J.-C. (1981). Phosphorylation of the caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases. Biochimie 63, 1-17.
91. Mercier, J.-C., Grosclaude, F. and Ribadeau-Dumas, B. (1971). Structure primaire de la caseine a bovine. Sequence complete. Eur. J. Biochem. 23, 41-51.
92. Mercier, J.-C., Brignon, G. and Ribadeau-Dumas, B. (1973). Structure primarie de la caseine K-bovine B. Sequence complete. Eur. J. Biochem. 35, 222-235.
93. Mikheeva, L.M., Grinberg, N.V., Grinberg, V.Ya., Khokhlov, A.R. and De Kruif, C.G. (2003). Thermodynamics of micellization of bovine ß-casein by high-sensitivity differential scanning calorimetry. Langmuir 19, 2913-2921.
94. Minkiewicz, P., Slangen, C.J., Lagerwerf, F.M., Haverkamp, J., Rollema, H.S. and Visser, S. (1996). Reversed-phase high-performance liquid chromatographic separation of bovine K-casein macropeptide and characterization of isolated fractions. J. Chrom. A 743, 123-135.
95. Miranda, G., Anglade, P., Mahe, M.-F. and Erhardt, G. (1993). Biochemical characterization of the bovine genetic kappa-casein C and E variants. Anim. Genet. 4, 27-31.
96. Molle, D. and Leonil, J. (1995). Heterogeneity of the bovine K-casein caseino-macropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry. J.Chrom. A 708, 223-230.
97. Ng-Kwai-Hang, K.F. and Grosclaude, F. (2003). Genetic polymorphism of milk proteins, in Advanced Dairy Chemistry 1: proteins, 3rd edn., P.F Fox and P.L.H. McSweeney, eds., Kluwer Acedemic/Plenum Publishers, New York. pp 739-816.
98. Ng-Kwai-Hang, K.F., Hayes, J.F., Moxley, J.E. and Monardes, H.G. (1984). Association of genetic variants of casein and milk serum proteins with milk, fat, and protein production by dairy cattle. J. Dairy Sci. 67, 835-840.
99. Niki, V.R., Takase, K. and Arima, S. (1977). Über die gestalt and größe des temperaturabhängigen assoziats von ß-casein. Milchwissenschaft 32, 577-582.
100. Noelken, M. and Reibstein, M. (1968). The conformation of ß-casein B. Arch. Biochem. Biophys. 123, 397.
101. O’Connell, J.E., Grinberg, V.Ya. and De Kruif, C.G. (2003). Association behavior of ß-casein. J. Colloid Interf. Sci. 258, 33-39.
102. Ono, T., Kaminogawa, S., Odagiri, S. and Yamauchi, K. (1976). A study on the binding of calcium ions to a-casein. Agric. Biol. Chem. 40, 1717-1723.
103. Ono, T., Yahagi, M. and Odagiri, S. (1980). The binding of calcium to K-casein and para-K-casein. Agric. Biol. Chem. 44, 1499-1503.
104. Ono T., Yada, R., Yunati, K. and Nakai, S. (1987). Comparison of the comformations of K-casein, K-casein and glycomacropeptide. Biochim. Biophys. Acta. 911,318-325.
105. Osta, R., Marcos, S. and Rodellar, C. (1995). A MnlI polymorphism at the bovine as2-casein gene. Anim. Genet. 26, 213.
106. Parker, T.G. and Dalgleish, D.G. (1981). Binding of calcium ions to bovine b-casein. J. Dairy Res. 48, 71-76.
107. Parry, R.M. and Carroll, R.J. (1969). Location of K-casein in milk micelles. Biochim. Biophys. Acta 194, 138-150.
108. Payens, T.A.J. and Heremans, K. (1969). Effect of pressure on the temperature-dependent association of b-casein. Biopolymers 8, 335-345.
109. Payens, T.A.J. and Schmidt, P.G. (1965). The thermodynamic parameters of the association of as1-casein C. Biochim. Biophys. Acta 109, 214-222.
110. Payens, T.A.J. and Schmidt, D.G. (1966). Boundary spreading of rapidly polymerizing as 1-casein B and C during sedimentation. Arch. Biochem. Biophys. 115, 136-145.
111. Payens, T.A.J. and Van Markwijk, B.W. (1963). Some features of the association of b-casein. Biochim. Biophys. Acta 71, 517-530.
112. Payens, T.A.J., Brinkhuis, J.A. and Van Markwijk, B.W. (1969). Self-association in non-ideal systems. Combined light scattering and sedimentation measurements in b-casein solutions. Biochim. Biophys. Acta 175, 434-437.
113. Pepper, L. and Farrell, H.M. Jr. (1982). Interactions leading to formation of casein submicelles. J. Dairy Sci. 65, 2259-2266.
114. Pisano, A., Packer, N.H., Redmond, J.W., Williams, K.L. and Gooley, A.A. (1994). Characterization of O-linked glycosylation motifs in the glycopeptides domain of bovine K-casein. Glycobiology 4, 837-844.
115. Prinzenberg, E.-M., Hiendleder, S., Ikonen, T. and Erhardt, G. (1996). Molecular genetic characterization of new bovine K-casein alleles CSN3-F and CSN3-G and genotyping by PCR-RFLP. Anim. Genet. 27, 347-349.
116. Prinzenberg, E.-M., Krause, I. and Erhardt, G. (1999). SCCP analysis of the bovine CSN3 locus discriminates six alleles corresponding to known protein variants (A, B, C, E, F, G) and three new DNA polymorphism (H, I, A1). Anim. Biotechnol. 10, 49-62.
117. Qi, P.X., Wickham, E.D. and Farrell, H.M. Jr. (2004). Thermal and alkaline denaturation of bovine b-casein. Prot. J. 23, 389-402.
118. Qi, P.X., Wickham, E.D., Piotrowski, E.G., Fagerquist, C.K. and Farrell, H.M. Jr. (2005). Implication of C-terminal deletion on the structure and stability of bovine b-casein. Prot. J. 24, 431-444.
119. Raap, J., Kerling, K.E.T., Vreeman, H.J. and Visser, S. (1983). Peptide substrates for chymosin (rennin): conformational studies of K-casein-related oligopeptides by circular dichroism and secondary structure prediction. Arch. Biochem. Biophys. 221, 117-124.
120. Rasmussen, L.K., Hojrup, P. and Petersen, T.E. (1992). Localization of two interchain disulfide bridges in dimers of bovine aS2-casein. Eur. J. Biochem. 203, 381-386.
121. Rasmussen, L.K., Hojrup, P. and Petersen, T.E. (1994). Disulphide arrangement in bovine caseins: localization of intrachain disulphide bridges in monomers of k-and as2-casein from bovine milk. J. Dairy Res. 61, 485-493.
122. Ribadeau-Dumas, B., Grosclaude, F. and Mercier, J.-C. (1970). Localization in the peptide chain of bovine beta casein of the His-Gln substitution differentiating the A2 and A3 genetic variants. CR Acad. Sci. D: Sci. Natur. 270, 2369-2372.
123. Ribadeau-Dumas, B., Brignon, G., Grosclaude, F. and Mercier, J.-C. (1972). Structure primaire de la casein b bovine. Eur. J. Biochem. 25, 505-514
124. Rollema, H.S., Brinkhuis, J.A. and Vreeman, H.J. (1988) 1H-NMR studies of bovine kappa-casein and casein micelles. Neth. Milk Dairy J. 42, 233-248.
125. Saito, T. and Itoh, T. (1992). Variations and distributions of O-glycosidically linked sugar chains in bovine K-casein. J. Dairy Sci. 75, 1768-1774.
126. Sawyer, L. and Holt, C. (1993). The secondary structure of milk proteins and their biological function. J. Dairy Sci. 76, 3062-3078.
127. Schmidt, D.G. (1969). On theAssociation of as]-Casein, Ph.D. Thesis, University of Utrecht.
128. Schmidt, D.G. (1970a). Differences between the association of the genetic variants B, C and D of as 1-casein. Biochim. Biophys. Acta 221, 140-142.
129. Schmidt, D.G. (1970b). The association of as1-casein B at pH 6.6. Biochim. Biophys. Acta 207,130-138.
130. Schmidt, D.G. (1982). Association of caseins and casein micelle structure, in, Developments in Dairy Chemistry1, P.F. Fox, ed., Elsevier Applied Science, London.pp 61-86.
131. Schmidt, D.G. and Payens, T.A.J. (1972). The evaluation of positive and negative contributions to the second virial coefficient of some milk proteins. J. Coll. Interface Sci. 39, 655-662.
132. Schmidt, D.G. and Van Markwijk, B.W. (1968). Further studies on the associating subunit of as1-casein. Biochim. Biophys. Acta 154, 613-614.
133. Senocq, D., Molle, D., Pochet, S., Leonil, J., Dupont, D. and Levieux, D. (2002). A new bovine b-casein genetic variant characterized by a Met93^Leu93 substitution in the sequence A2. Lait 82, 171-180.
134. Smyth, E., Syme, C.D., Blanch, E.W., Hecht, L., Vasak, M. and Barron, L.D. (2001). Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers 58, 138-151.
135. Snoeren, T.H.M., Van Markwijk, B. and Van Montfort, R. (1980). Some physicochemical properties of bovine as2-casein. Biochim. Biophys. Acta 622, 266-276.
136. Stewart, A.F., Bonsing, J., Beattie, C.W., Shah, F., Willis, M. and Mackinlay, A.G. (1987). Complete nucleotide sequences of bovine as2-and b-casein cDNAs: comparisons with related sequences in other species. 4 231_241.
137. Sulimova, G.E., Sokolova, S.S., Semikozova, O.P., Nguet, M. and Berberov, E.M. (1992). Analysis of DNA polymorphisms of clustered genes in cattle: casein genes and genes of the major histocompatibility complex (BOLA). Tsitol. I Genetika 26, 18-26.
138. Swaisgood, H. E. (1982). Chemistry of milk proteins, in, Developments in Dairy Chemistry 1: Proteins. P.F. Fox, ed., Applied Science Publishers, New York. pp 1-59.
139. Swaisgood, H.E. (1992). Chemistry of the caseins, in, Advanced Dairy Chemistry 1: Proteins, 2nd edn. P.F. Fox, ed., Elsevier Applied Science, New York. pp 63-110.
140. Swaisgood, H.E. (2003). Chemistry of caseins, in, Advanced Dairy Chemistry 1: Proteins, 3rd edn. P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic/Plenum Publishers, New York. pp 139-201.
141. Swaisgood, H.E. and Timasheff, S.N. (1968). Association of as1-casein C in the alkaline pH range. Arch. Biochem. Biophys. 125, 344-361.
142. Swaisgood, H.E., Brunner, J.R. and Lillevik, H.A. (1964). Physical parameters of K-casein from cow’s milk. Biochem. 3, 1616-23.
143. Syme, C.D., Blanch, E.W., Holt, C., Jakes, R., Goedert, M., Hecht, L. and Barron, L.D. (2002). A Raman optical activity study of rheomorphism in casein, synucleins and tau. New insight into the structure and behavior of natively unfolded proteins. Eur. J. Biochem. 269, 148-156.
144. Tai, M.-S. and Kegeles, G. (1984). A micelle model for the sedimentation behavior of bovine b-casein. Biophys. Chem. 20, 81-87.
145. Takase, K., Niki, R. and Arima, S. (1980). A sedimentation equilibrium study of the temperature-dependent association of bovine b-casein. Biochim. Biophys. Acta 622, 1-8.
146. Talbo, G.H., Suckau, D., Malkoski, M. and Reynolds, E.C. (2001). MALDI-PSD-MS analysis of the phosphorylation sites of caseinomacropeptide. Peptides 22, 1093-1098.
147. Talbot, B. and Waugh, D.F. (1970). Micelle-forming characteristics of monomeric and covalent polymeric K-caseins. Biochem. 9, 2807-2813.
148. Tanford C. (1962). Contribution of hydrophobic interactions to the stability of the globular conformation of proteins. J. Am. Chem. Soc. 84, 4240-4274.
149. Tauzin, J., Miclo, L., Roth, S., Molle, D. and Gaillard, -L. (2003). Tryptic hydrolysis of bovine as2-casein: identification and release kinetics of peptides. Int. Dairy J. 13, 15-27.
150. Thompson, M.P. and Farrell, H.M. Jr. (1974). Genetic variants of the milk proteins, in, Lactation, Vol. III, B.L. Larson and V.R. Smith, eds., Academic, New York. pp 109-134.
151. Thompson, M.P., Kalan, E.B. and Greenberg, R. (1967). Properties of caseins modified by treatment with carboxypeptidase A. J. Dairy Sci. 50,767-769.
152. Thorn, D.C., Meehan, S., Sunde, M., Rekas, A., Gras, S.L., MacPhee, C.E., Dobson, C.M., Wilson, M.R. and Carver, J.A. (2005). Amyloid fibril formation by bovine milk K-casein and its inhibition by the molecular chaperones a-and b-casein. Biochem 44, 17027-17036.
153. Thorn, D.C., Ecroyd, H., Sunde, M., Poon, S. and Carver, J.A. (2008). Amyloid fibril formation by bovine milk as2-casein occurs under physiological conditions yet is prevented by its natural counterpart, as 1-casein. Biochem. 47, 3926-3936.
154. Thurn, A., Burchard, W. and Niki, R. (1987). Structure of casein micelles. I. Small angle neutron scattering and light scattering from b-casein and K-casein. Colloid Polymer Sci. 265, 653-666.
155. Toma, S.J. and Nakai, S. (1973). Calcium sensitivity and molecular-weight of casein-as5. J. Dairy Sci. 56, 1559-1562.
156. Trieu-Cuot, P. and Gripon J.-C. (1981). Electrofocusing and two-dimensional electrophoresis of bovine caseins. J. Dairy Res. 48, 303-310.
157. Visser, S., Slangen, C.J., Lagerwerf, F.M., Van Dongen, W.S. and Haverkamp, J. (1995). Identification of a new variant of bovine beta-casein using reversed-phase high-performance liquid-chromatography and mass-spectrometric analysis. J. Chrom. A 711, 141-150.
158. Vreeman, H.J. (1979). The association of bovine SH-K-casein at pH 7.0. J. Dairy Res. 46, 271-276.
159. Vreeman, H.J., Both, P., Brinkhuis, J.A. and Van der Spek, C. (1977). Purification and some physicochemical properties of bovine K-casein. Biochim. Biophys. Acta 491, 93-103.
160. Vreeman, H.J., Brinkhuis, J.A. and Van der Spek, C. (1981). Some association properties of bovine SH-k-casein. Biophys. Chem. 14, 185-193.
161. Vreeman, H.J., Visser, S., Slangen, C.J. and Van Riel, J.A.M. (1986). Characterization of bovine K-casein fraction and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high-performance gel-permeation chromatography. Biochem. J. 240, 87-97.
162. Whitney, R.M., Brunner, J.R., Ebner, K.E., Farrell, H.M. Jr., Josephson, R.V., Morr, C.V. and Swaisgood, H.E. (1976). Nomenclature of the proteins of cow’s milk: fourth revision. J. Dairy Sci. 59, 795-815.
163. Yamuachi, K., Takemoto, S. and Tsugo, T. (1967). Calcium-binding property of dephosphorylated casein. Agric. Biol. Chem. 31, 54-63.
164. Yan, S.-C.B. and Wold, F. (1984). Neoglycoproteins: in vitro introduction of glycosyl units at glutamines in b-casein using transglutaminase. Biochem. 23, 3759-3765.