Post-Translational Modifications of Caseins

Milk Proteins

Volumn , Issue , 2008, Pages 107-132

  Holland, John W ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84882463554     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374039-7.00004-0     Document Type: Chapter

References (129)

1. Addeo F., Martin P., Ribadeau-Dumas B. Susceptibility of buffalo and cow κ-caseins to chymosin action. Milchwissenschaft 1984, 39:202-205.
2. Alais C., Jolles P. Comparative study of the caseinoglycopeptides formed by the action of rennin on caseins from the cow, sheep and goat, II, Study of the non-peptide portion. Biochimica et Biophysica Acta 1961, 51:315-322.
3. Alexander L.J., Stewart A.F., Mackinlay A.G., Kapelinskaya T.V., Tkach T.M., Gorodetsky S.I. Isolation and characterization of the bovine κ-casein gene. European Journal of Biochemistry 1988, 178:395-401.
4. Belloque J., Villamiel M., Lopez F.R., Olano A. Release of galactose and N-acetylglucosamine during the storage of UHT milk. Food Chemistry 2001, 72:407-412.
5. Bobe G., Beitz D.C., Freeman A.E., Lindberg G.L. Effect of milk protein genotypes on milk protein composition and its genetic parameter estimates. Journal of Dairy Science 1999, 82:2797-2804.
6. Bodenmiller B., Mueller L.N., Mueller M., Domon B., Aebersold R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nature Methods 2007, 4:231-237.
7. Bouguyon E., Beauvallet C., Huet J.-C., Chanat E. Disulphide bonds in casein micelle from milk. Biochemical and Biophysical Research Communications 2006, 343:450-458.
8. s2-casein D is generated by exon VIII skipping. Gene 1993, 128:289-293.
9. Bovenhuis H., Van Arendonk J.A., Korver S. Associations between milk protein polymorphisms and milk production traits. Journal of Dairy Science 1992, 75:2549-2559.
10. Brody E.P. Biological activities of bovine glycomacropeptide. British Journal of Nutrition 2000, 84(Suppl 1):S39-S46.
11. Cases E., Vidal V., Cuq J.L. Effect of κ-casein deglycosylation on the acid coagulability of milk. Journal of Food Science 2003, 68:2406-2410.
12. Chabance B., Jolles P., Izquierdo C., Mazoyer E., Francoual C., Drouet L., Fiat A.M. Characterization of an antithrombotic peptide from κ-casein in newborn plasma after milk ingestion. British Journal of Nutrition 1995, 73:583-590.
13. Chaplin B., Green M.L. Determination of the proportion of κ-casein hydrolyzed by rennet on coagulation of skim-milk. Journal of Dairy Research 1980, 47:351-358.
14. Choi J.W., Ng-Kwai-Hang K.F. Effects of genetic variants of κ-casein and beta-lactoglobulin and heat treatment on coagulating properties of milk. Asian-Australasian Journal of Animal Sciences 2003, 16:1212-1217.
15. Clare D.A., Swaisgood H.E. Bioactive milk peptides: a prospectus. Journal of Dairy Science 2000, 83:1187-1195.
16. Claverol S., Burlet-Schiltz O., Gairin J.E., Monsarrat B. Characterization of protein variants and post-translational modifications: ESI-MSn analyses of intact proteins eluted from polyacrylamide gels. Molecular and Cellular Proteomics 2003, 2:483-493.
17. Collins M.O., Yu L., Choudhary J.S. Analysis of protein phosphorylation on a proteome-scale. Proteomics 2007, 7:2751-2768.
18. Coolbear K.P., Elgar D.F., Ayers J.S. Profiling of genetic variants of bovine k-casein macropeptide by electrophoretic and chromatographic techniques. International Dairy Journal 1996, 6:1055-1068.
19. Cox D.M., Zhong F., Du M., Duchoslav E., Sakuma T., McDermott J.C. Multiple reaction monitoring as a method for identifying protein post-translational modifications. Journal of Biomolecular Techniques 2005, 16:83-90.
20. Dalgleish D.G. Glycosylated κ-caseins and the sizes of bovine casein micelles. Analysis of the different forms of κ-casein. Biochimica et Biophysica Acta 1985, 830:213-215.
21. Dalgleish D.G. Analysis by fast protein liquid chromatography of variants of κ-casein and their relevance to micellar structure and renneting. Journal of Dairy Research 1986, 53:43-51.
22. Dalgleish D.G., Horne D.S., Law A.J.R. Size-related differences in bovine casein micelles. Biochimica et Biophysica Acta 1989, 991:383-387.
23. Dall'Olio F., Chiricolo M. Sialyltransferases in cancer. Glycoconjugate Journal 2001, 18:841-850.
24. Datta N., Deeth H.C. Age gelation of UHT milk-a review. Food and Bioproducts Processing 2001, 79:197-210.
25. Davies D.T., Law A.J.R. Variation in protein composition of bovine casein micelles and serum casein in relation to casein micelle size and milk temperature. Journal of Dairy Research 1983, 50:67-75.
26. Doi H., Kawaguchi N., Ibuki F., Kanamori M. Susceptibility of κ-casein components to various proteases. Journal of Nutritional Science and Vitaminology (Tokyo) 1979, 25:33-41.
27. Doi H., Kobatake H., Ibuki F., Kanamori M. Attachment sites of carbo-hydrate portions to peptide chain of κ-casein from bovine colostrum. Agricultural and Biological Chemistry 1980, 44:2605-2611.
28. Donnelly W.J., McNeill G.P., Buchheim W., McGann T.C. A comprehensive study of the relationship between size and protein composition in natural bovine casein micelles. Biochimica et Biophysica Acta 1984, 789:136-143.
29. Dziuba J., Minikiewicz P. Influence of glycosylation on micelle-stabilising ability and biological properties of C-terminal fragments of cow's κ-casein. International Dairy Journal 1996, 6:1017-1044.
30. Erhardt, G., Prinzenberg, E-M., Buchberger, J., Krick-Salek, H., Krause, I. and Miller, M. (1997). Bovine κ-casein G: detection, occurrence, molecular genetic characterisation, genotyping and coagulation properties, In Milk Protein Polymorphism, IDF Special Issue 9702, pp. 328-29. Brussels: International Dairy Federation.
31. Farrell H.M., Cooke P.H., Wickham E.D., Piotrowski E.G., Hoagland P.D. Environmental influences on bovine κ-casein: reduction and conversion to fibrillar (amyloid) structures. Journal of Protein Chemistry 2003, 22:259-273.
32. Farrell H.M., 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., Swaisgood H.E. Nomenclature of the proteins of cows' milk - sixth revision. Journal of Dairy Science 2004, 87:1641-1674.
33. Ferranti P., Pizzano R., Garro G., Caira S., Chianese L., Addeo F. Mass spectrometry-based procedure for the identification of ovine casein heterogeneity. Journal of Dairy Research 2001, 68:35-51.
34. Fiat A.M., Jolles J., Loucheux-Lefebvre M.H., Alais C., Jolles P. Localisation of the prosthetic sugar groups of bovine colostrum κ-casein. Hoppe Seylers Zeitschrift fur Physiologische Chemie 1981, 362:1447-1454.
35. Fiat A.M., Chevan J., Jolles P., De Waard P., Vliegenthart J.F., Piller F., Cartron J.P. Structural variability of the neutral carbohydrate moiety of cow colostrum κ-casein as a function of time after parturition. Identification of a tetrasaccharide with blood group I specificity. European Journal of Biochemistry 1988, 173:253-259.
36. FitzGerald, R. J. Hill, J. P. (1997) The relationship between milk protein polymorphismand the manufacture and functionality of dairy products. In Milk Protein Polymorphism, IDF Special Issue 9702, pp. 355-71. Brussels: International Dairy Federation.
37. Fournet B., Fiat A.M., Montreuil J., Jolles P. The sugar part of κ-caseins from cow milk and colostrum and its microheterogeneity. Biochimie 1975, 57:161-165.
38. Fournet B., Fiat A.M., Alais C., Jolles P. Cow κ-casein: structure of the carbohydrate portion. Biochimica et Biophysica Acta 1979, 576:339-346.
39. Ginger M.R., Grigor M.R. Comparative aspects of milk caseins. Comparative Biochemistry and Physiology B 1999, 124:133-145.
40. Girardet J-M., Miclo L., Florent S., Mollé D., Gaillard J-L. Determination of the phosphorylation level and deamidation susceptibility of equine β-casein. Proteomics 2006, 6:3707-3717.
41. Gorodetskii S.I., Kershulite D.R., Korobko V.G. Primary structure of cDNA of Bos taurus κ-casein macropeptide. Bioorganicheskaya Khimiya 1983, 9:1693-1695.
42. Greenberg R., Groves M.L., Dower H.J. Human β-casein. Amino acid sequence and identification of phosphorylation sites. Journal of Biological Chemistry 1984, 259:5132-5138.
43. Grosclaude F., Mahe M.F., Mercier J.C., Ribadeau-Dumas B. Characterization of genetic variants of α-s1 and β bovine caseins. European Journal of Biochemistry 1972, 26:328-337.
44. Grosclaude F., Mahe M-F., Mercier J-C., Ribadeau-Dumas B. Localization of amino-acid substitutions that differenciate bovine κ-casein variants A and B. Annales de Genetique et de Selection Animale 1972, 4:515-521.
45. Groves M.L., Dower H.J., Farrell H.M. Re-examination of the polymeric distributions of κ-casein isolated from bovine milk. Journal of Protein Chemistry 1992, 11:21-28.
46. Groves M.L., Wickham E.D., Farrell H.M. Environmental effects on disulfide bonding patterns of bovine κ-casein. Journal of Protein Chemistry 1998, 17:73-84.
47. Guerin J., Alais C., Jolles J., Jolles P. κ-casein from bovine colostrum. Biochimica et Biophysica Acta 1974, 351:325-332.
48. Guyomarc'h F., Law A.J., Dalgleish D.G. Formation of soluble and micelle-bound protein aggregates in heated milk. Journal of Agricultural and Food Chemistry 2003, 51:4652-4660.
49. Holland J.W., Deeth H.C., Alewood P.F. Proteomic analysis of κ-casein micro-heterogeneity. Proteomics 2004, 4:743-752.
50. Holland J.W., Deeth H.C., Alewood P.F. Analysis of O-glycosylation site occupancy in bovine κ-casein glycoforms separated by two-dimensional gel electro-phoresis. Proteomics 2005, 5:990-1002.
51. Holland J.W., Deeth H.C., Alewood P.F. Resolution and characterisation of multiple isoforms of bovine κ-casein by 2-DE following a reversible cysteine-taggingenrichment strategy. Proteomics 2006, 6:3087-3095.
52. Holland J.W., Deeth H.C., Alewood P.F. Analysis of disulfide linkages in bovine κ-casein oligomers using 2-dimensional electrophoresis. Electrophoresis 2008, 29:2402-2410.
53. Holt C., Horne D.S. The hairy casein micelle: evolution of the concept and its implications for dairy technology. Netherlands Milk and Dairy Journal 1996, 50:85-111.
54. Horne D.S. Casein interactions: casting light on the black boxes, the structure in dairy products. International Dairy Journal 1998, 8:171-177.
55. Horne D.S. Casein structure, self-assembly and gelation. Current Opinion in Colloid and Interface Science 2002, 7:456-461.
56. Ibeagha-Awemu E.M., Prinzenberg E.M., Jann O.C., Luhken G., Ibeagha A.E., Zhao X., Erhardt G. Molecular characterization of bovine CSN1S2*B and extensive distribution of zebu-specific milk protein alleles in European cattle. Journal of Dairy Science 2007, 90:3522-3529.
57. Jolles J., Fiat A.M., Alais C., Jolles P. Comparative study of cow and sheep κ-caseinoglycopeptides: determination of the N-terminal sequences with a sequencer and location of the sugars. FEBS Letters 1973, 30:173-176.
58. Kanamori M., Kawaguchi N., Ibuki F., Doi H. Attachment sites of carbo-hydrate moieties to peptide chain of bovine κ-casein from normal milk. Agricultural and Biological Chemistry 1980, 44:1855-1861.
59. Kanamori M., Doi H., Ideno S., Ibuki F. Presence of O-glycosidic linkage through serine residue in κ-casein component from bovine mature milk. Journal of Nutritional Science and Vitaminology (Tokyo) 1981, 27:231-241.
60. Kapkova P., Lattova E., Perreault H. Nonretentive solid-phase extraction of phosphorylated peptides from complex peptide mixtures for detection by matrix-assisted laser desorption/ionization mass spectrometry. Analytical Chemistry 2006, 78:7027-7033.
61. Keating A.F., Davoren P., Smith T.J., Ross R.P., Cairns M.T. Bovine k-casein gene promoter haplotypes with potential implications for milk protein expression. Journal of Dairy Science 2007, 90:4092-4099.
62. Kilara A., Panyam D. Peptides from milk proteins and their properties. Critical Reviews in Food Science and Nutrition 2003, 43:607-633.
63. Leaver J., Horne D.S. Chymosin-catalysed hydrolysis of glycosylated and nonglycosylated bovine κ-casein adsorbed on latex particles. Journal of Colloid and Interface Science 1996, 181:220-224.
64. Ledoux N., Mahé S., Dubarry M., Bourras M., Benamouzig R., Tomé D. Intraluminal immunoreactive caseinomacropeptide after milk protein ingestion in humans. Nahrung 1999, 43:196-200.
65. Li E.W.Y., Mine Y. Immunoenhancing effects of bovine glycomacropeptide and its derivatives on the proliferative response and phagocytic activities of human macrophagelike cells, U937. Journal of Agricultural and Food Chemistry 2004, 52:2704-2708.
66. Lodes A., Krause I., Buchberger J., Aumann J., Klostermeyer H. The influence of genetic variants of milk proteins on the composition and technological properties of milk. 1. Casein micelle size and the content of non-glycosylated κ-casein. Milchwissenschaft 1996, 51:368-373.
67. s1-casein H and κ-casein. Genetics Selection Evolution 1999, 31:239-253.
68. Malkoski M., Dashper S.G., O'Brien-Simpson N.M., Talbo G.H., Macris M., Cross K.J., Reynolds E.C. Kappacin, a novel antibacterial peptide from bovine milk. Antimicrobial Agents and Chemotherapy 2001, 45:2309-2315.
69. s1 casein. European Journal of Biochemistry 1977, 78:411-417.
70. Marin A., Mawhinney T.P., Marshall R.T. Glycosidic activities of Pseudomonas fluorescens on fat-extracted skim milk, buttermilk, and milk fat globule membranes. Journal of Dairy Science 1984, 67:52-59.
71. Martin P., Szymanowska M., Zwierzchowski L., Leroux C. The impact of genetic polymorphisms on the protein composition of ruminant milks. Reproduction Nutrition Development 2002, 42:433-459.
72. McGann T.C., Donnelly W.J., Kearney R.D., Buchheim W. Composition and size distribution of bovine casein micelles. Biochimica et Biophysica Acta 1980, 630:261-270.
73. Mercier J.C. Phosphorylation of caseins, present evidence for an amino acid triplet code post-translationally recognized by specific kinases. Biochimie 1981, 63:1-17.
74. Mercier J.C., Brignon G., Ribadeau-Dumas B. Primary structure of bovine κ B casein. Complete sequence. European Journal of Biochemistry 1973, 35:222-235.
75. Miclo L., Girardet J.M., Egito A.S., Molle D., Martin P., Gaillard J.L. The primary structure of a low-M(r) multiphosphorylated variant of β-casein in equine milk. Proteomics 2007, 7:1327-1335.
76. Minkiewicz P., Dziuba J., Muzinska B. The contribution of N-acetylneuraminicacid in the stabilization of micellar casein. Polish Journal of Food and Nutrition Sciences 1993, 2:39-48.
77. Miranda G., Anglade P., Mahe M.F., Erhardt G. Biochemical characterization of the bovine genetic κ-casein C and E variants. Animal Genetics 1993, 24:27-31.
78. Molle D., Leonil J. Heterogeneity of the bovine κ-casein caseinomacro-peptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry. Journal of Chromatography A 1995, 708:223-230.
79. Neveu C., Molle D., Moreno J., Martin P., Leonil J. Heterogeneity of caprine β-casein elucidated by RP-HPLC/MS: genetic variants and phosphorylations. Journal of Protein Chemistry 2002, 21:557-567.
80. Ng-Kwai-Hang, K. F. (1997). A review of the relationship between milk protein polymorphism and milk composition/milk production, In Milk Protein Polymorphism, IDF Special Issue 9702, pp. 22-37. Brussels: International Dairy Federation.
81. O'Connell J.E., Fox P.F. The two-stage coagulation of milk proteins in the minimum of the heat coagulation time-pH profile of milk: effect of casein micelle size. Journal of Dairy Science 2000, 83:378-386.
82. O'Connell, J. E. and Fox, P. F. (2003). Heat-induced coagulation of milk. In Advanced Dairy Chemistry, Volume 1, Protein, 3rd edn (P. F. Fox and P. L. H. McSweeney, eds) pp. 879-945. New York: Kluwer Academic/Plenum Publishers.
83. O'Donnell R., Holland J.W., Deeth H.C., Alewood P. Milk proteomics. International Dairy Journal 2004, 14:1013-1023.
84. Pisano A., Packer N.H., Redmond J.W., Williams K.L., Gooley A.A. Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine κ-casein. Glycobiology 1994, 4:837-844.
85. Prinzenberg E.M., Hiendleder S., Ikonen T., Erhardt G. Molecular genetic characterization of new bovine κ-casein alleles CSN3F and CSN3G and geno-typing by PCR-RFLP. Animal Genetics 1996, 27:347-349.
86. Prinzenberg E.M., Krause I., Erhardt G. SSCP analysis at the bovine CSN3 locus discriminates six alleles corresponding to known protein variants (A, B, C, E, F, G) and three new DNA polymorphisms (H, I, A1). Animal Biotechnology 1999, 10:49-62.
87. Rasmussen L.K., Hojrup P., Petersen T.E. The multimeric structure and disulfide-bonding pattern of bovine κ-casein. European Journal of Biochemistry 1992, 207:215-222.
88. s2-casein from bovine milk. Journal of Dairy Research 1994, 61:485-493.
89. Rasmussen L.K., Sorensen E.S., Petersen T.E., Nielsen N.C., Thomsen J.K. Characterization of phosphate sites in native ovine, caprine, and bovine casein micelles and their caseinomacropeptides: a solid-state phosphorus-31 nuclear magnetic resonance and sequence and mass spectrometric study. Journal of Dairy Science 1997, 80:607-614.
90. Rasmussen L.K., Johnsen L.B., Tsiora A., Sorensen E.S., Thomsen J.K., Nielsen N.C., Jakobsen H.J., Petersen T.E. Disulphide-linked caseins and casein micelles. International Dairy Journal 1999, 9:215-218.
91. Recio M.I., Villamiel M., Martínez-Castro I., Olano A. Changes in free monosaccharides during storage of some UHT milks: a preliminary study. Zeitschrift für Lebensmitteluntersuchung und -Forschung A 1998, 207:180-181.
92. Riggs L., Sioma C., Regnier F.E. Automated signature peptide approach for proteomics. Journal of Chromatography A 2001, 924:359-368.
93. Robitaille G., Ayers C. Effects of κ-casein glycosylation on heat stability of milk. Food Research International 1995, 28:17-21.
94. Robitaille G., Ng-Kwai-Hang K.F., Monardes H.G. Variation of the N-acetylneuraminic acid content of bovine κ-casein. Journal of Dairy Research 1991, 58:107-114.
95. Robitaille G., Ng-Kwai-Hang K.F., Monardes H.G. Association of κ-casein glycosylation with milk production and composition in holsteins. Journal of Dairy Science 1991, 74:3314-3317.
96. Robitaille G., Ng-Kwai-Hang K.F., Monardes H.G. Effect of κ-casein glycosylation on cheese yielding capacity and coagulating properties of milk. Food Research International 1993, 26:365-369.
97. Rollema H.S. Casein association and micelle formation. Advanced Dairy Chemistry 1992, 111-140. Elsevier Applied Science, London. P.F. Fox (Ed.).
98. Saito T., Itoh T. Variations and distributions of O-glycosidically linked sugar chains in bovine κ-casein. Journal of Dairy Science 1992, 75:1768-1774.
99. Saito T., Itoh T., Adachi S. The chemical structure of a tetrasaccharide containing N-acetylglucosamine obtained from bovine colostrum κ-casein. Biochimica et Biophysica Acta 1981, 673:487-494.
100. Saito T., Itoh T., Adachi S., Suzuki T., Usui T. The chemical structure of neutral and acidic sugar chains obtained from bovine colostrum κ-casein. Biochimica et Biophysica Acta 1981, 678:257-267.
101. Saito T., Itoh T., Adachi S., Suzuki T., Usui T. A new hexasaccharide chain isolated from bovine colostrum κ-casein taken at the time of parturition. Biochimica et Biophysica Acta 1982, 719:309-317.
102. Sawyer W.H. Complex between β-lactoglobulin and κ-casein. A review. Journal of Dairy Science 1969, 52:1347-1355.
103. Schauer R. Achievements and challenges of sialic acid research. Glycoconjugate Journal 2000, 17:485-499.
104. Schild T.A., Wagner V., Geldermann H. Variants within the 5′-flankingregions of bovine milk-protein-encoding genes: I. κ-casein-encoding gene. Theoretical and Applied Genetics 1994, 89:116-120.
105. Schlieben S., Erhardt G., Senft B. Genotyping of bovine κ-casein (κ-CNA, κ-CNB, κ-CNC, κ-CNE) following DNA sequence amplification and direct sequencing of kappa-CNE PCR product. Animal Genetics 1991, 22:333-342.
106. Shekar P.C., Goel S., Rani S.D.S., Sarathi D.P., Alex J.L., Singh S., Kumar S. κ-Casein-deficient mice fail to lactate. Proceedings of the National Academy of Sciences of the USA 2006, 103:8000-8005.
107. Slattery C.W. Variation in the glycosylation pattern of bovine κ-casein with micelle size and its relationship to a micelle model. Biochemistry 1978, 17:1100-1104.
108. Smith, M. H., Hill, J. P., Creamer, L. K., and Plowman, J. E. (1997). Towards understanding the variant effect on the rate of cleavage by chymosin on κ-caseins A and C, In Milk Protein Polymorphism, IDF Special Issue 9702, pp. 185-88. Brussels: International Dairy Federation.
109. Smith M.H., Edwards P.J., Palmano K.P., Creamer L.K. Structural features of bovine caseinomacropeptide A and B by 1H nuclear magnetic resonance spectroscopy. Journal of Dairy Research 2002, 69:85-94.
110. Sulimova G.E., Sokolova S.S., Semikozova O.P., Nguet L.M., Berberov E.M. Analysis of DNA polymorphism of cluster genes in cattle: casein genes and major histocompatibility complex (MHC) genes. Tsitologiia i Genetika 1992, 26:18-26.
111. Sulimova G.E., Badagueva Iu.N., Udina I.G. Polymorphism of the κ-casein gene in populations of the subfamily Bovinae. Genetika 1996, 32:1576-1582.
112. Swaisgood, H. E. (2003). Chemistry of the caseins. In Advanced Dairy Chemistry, Volume 1, Proteins, 3rd edn (P. F. Fox and P. L. H. McSweeney, eds) pp. 139-202. New York: Kluwer Academic/Plenum Publishers.
113. Swaisgood H.E., Brunner J.R., Lillevik H.A. Physical parameters of κ-casein from cow's milk. Biochemistry 1964, 20:1616-1623.
114. Sweet S.M.M., Creese A.J., Cooper H.J. Strategy for the identification of sites of phosphorylation in proteins: neutral loss triggered electron capture dissociation. Analytical Chemistry 2006, 78:7563-7569.
115. Takeuchi M., Tsuda E., Yoshikawa M., Sasaki R., Chiba H. Fractionation and characterization of 9 subcomponents of bovine κ-casein A. Agricultural and Biological Chemistry 1985, 49:2269-2276.
116. Talbot B., Waugh D.F. Micelle-forming characteristics of monomeric and covalent polymeric κ-caseins. Biochemistry 1970, 9:2807-2813.
117. Ten Hagen K.G., Fritz T.A., Tabak L.A. All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 2003, 13:1R-16R.
118. van Halbeek H., Dorland L., Vliegenthart J.F., Fiat A.M., Jolles P. A 360-MHz 1H-NMR study of three oligosaccharides isolated from cow κ-casein. Biochimica et Biophysica Acta 1980, 623:295-300.
119. van Halbeek H., Dorland L., Vliegenthart J.F., Fiat A.M., Jolles P. Structural characterization of a novel acidic oligosaccharide unit derived from cow colostrum κ-casein. A 500MHz 1H-NMR study. FEBS Letters 1981, 133:45-50.
120. van Hooydonk A.C.M., Olieman C., Hagedoorn H.G. Kinetics of the chymosin-catalysed proteolysis of κ-casein in milk. Netherlands Milk and Dairy Journal 1984, 38:207-222.
121. van Hooydonk A.C.M., De Koster P.G., Boerrigter I.J. The renneting properties of heated milk. Netherlands Milk and Dairy Journal 1987, 41:3-18.
122. Vasbinder A.J., Alting A.C., Visschers R.W., De Kruif C.G. Texture of acid milk gels: formation of disulfide cross-links during acidification. International Dairy Journal 2003, 13:29-38.
123. Vreeman H.J., Visser S., Slangen C.J., Van Riel J.A. Characterization of bovine κ-casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high-performance gel-permeation chromatography. Biochemical Journal 1986, 240:87-97.
124. Walsh C.D., Guinee T.P., Reville W.D., Harrington D., Murphy J.J., O'Kennedy B.T., FitzGerald R.J. Influence of κ-casein genetic variant on rennet gel microstructure, Cheddar cheesemaking properties and casein micelle size. International Dairy Journal 1998, 8:707-714.
125. Walstra P. Casein sub-micelles: do they exist?. International Dairy Journal 1999, 9:189-192.
126. Wu H.Y., Tseng V.S., Liao P.C. Mining phosphopeptide signals in liquid chromatography-mass spectrometry data for protein phosphorylation analysis. Journal of Proteome Research 2007, 6:1812-1821.
127. Young W.W., Holcomb D.R., Ten Hagen K.G., Tabak L.A. Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family. Glycobiology 2003, 13:549-557.
128. Zevaco C., Ribadeau-Dumas B. A study on the carbohydrate binding sites of bovine κ-casein using high performance liquid chromatography. Milchwissenschaft 1984, 39:206-210.
129. Zhou H., Xu S., Ye M., Feng S., Pan C., Jiang X., Li X., Han G., Fu Y., Zou H. Zirconium phosphonate-modified porous silicon for highly specific capture of phosphopeptides and MALDI-TOF MS analysis. Journal of Proteome Research 2006, 5:2431-2437.