Biologically Active Factors in Bovine Milk and Dairy Byproducts: Influence on Cell Culture

Critical Reviews in Food Science and Nutrition

Volumn 37, Issue 4, 1997, Pages 393-410

  Guimont, C ^a   Marchall, E ^a   Girardet, J M ^a   Linden, G ^a  

^a UNIVERSITÉ DE LORRAINE   (France)

Author keywords

Bovine milk; Cell culture; Mitogenic factors; Serum; Whey proteins

Indexed keywords

BOVINAE; MAMMALIA;

MILK PROTEIN;

ANIMAL; CATTLE; CELL CULTURE; CELL DIVISION; CHEMISTRY; CULTURE MEDIUM; DAIRY PRODUCT; HUMAN; MILK; REVIEW;

ANIMALS; CATTLE; CELL DIVISION; CELLS, CULTURED; CULTURE MEDIA; DAIRY PRODUCTS; HUMANS; MILK; MILK PROTEINS;

EID: 0031160118     PISSN: 10408398     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408399709527780     Document Type: Article

References (176)

1. Lönnerdal, B., Biochemistry and physiological function of human milk proteins, Am. J. Clin. Nutr., 1985; 42: 1299-1317.
2. Koldowsky, O. and Thornburg, W., Hormones in milk, J. Pediatr. Gastroenterol. Nutr., 1987; 9: 172-196.
3. Read, L. C., Milk growth factors. In: Cockburn, F., Ed., Fetal and Neonatal Growth. John Wiley & Sons, London, 1988; 131-152.
4. Britton, J. and Kastin, A. J., Biologically active polypeptides in milk, Am. J. Med. Sci., 1991; 301: 124-132.
5. Grosvenor, C. E., Picciano, M. F., and Baumrucker, G. R., Hormones and growth factors in milk, Endrocin. Rev., 1993; 14: 10-28.
6. Muller, R., Mumberg, D., and Lucibello, F. C., Signals and genes in the control of cell-cycle progression, Biochem. Biophys. Acta, 1993; 1155: 151-179.
7. McAteer, J. A. and Davis, J., Basic cell culture technique and the maintenance of cell line. In: Davis, J. M., Ed., Basic Cell Culture. A Practical Approach. IRL Press, Oxford, 1994; 93-148.
8. Mossman, J., Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays, J. Immunol. Methods, 1983; 65: 1-2, 55-63.
9. Landegren, U., Measurement of cell numbers by means of the endogenous enzyme hexosaminidase. Application to detection of lymphokines, J. Immunol. Methods, 1984; 67: 379-388.
10. Basergha, R., Measuring parameters of growth. In: Basergha, R., Ed., Cell Growth and Division. A Practical Approach. IRL Press, Oxford, 1989; 1-16.
11. Iacopetta, B. J., Grieu, F., Horisberger, M., and Sunahara, G. I., Epidermal growth factor in human and bovine milk, Acta Paediatr., 1992; 81; 287-291.
12. Mroczkowski, B. and Reich, M., Identification of biologically active epidermal growth factor precursor in human fluids and secretions, Endocrinology, 1993; 132: 417-425.
13. Oka, Y., Gishan, F.K., Greene, H.L., and Orth, D.N., Effect of mouse epidermal growth factor/urogastrone on the functional maturation of rat intestine, Endocrinology, 1983; 112: 940-944.
14. Dembiski, A. B. and Johnson, L. R., Effect of epidermal growth factor on the development of rat gastric mucosa, Endocrinology, 1985; 116: 90-94.
15. Takizawa, H., Studies on the regulation of normal bronchial epithelial cell proliferation and proto-oncogene expression, Nippon Kyobu Shikkan Gakkai Zasshi, 1992, 30(Suppl.): 27-32.
16. Adamson, E. D., Dellar, M. J., and Warshaw, J. B., Functional EGF receptors are present on mouse embryo tissues, Nature (London), 1981; 291: 656-659.
17. Lorenzo, P. L., Illera, M. J., and Illera, M., Enhancement of cumulus expansion and nuclear maturation during bovine oocyte maturation in vitro by the addition of epidermal growth factor and insulin-like growth factor, J. Repod. Fertil., 1994; 101: 697-701.
18. Gong, J. C., McBride, D., Bramley, T. A., and Webb, R., Effects of recombinant bovine somatotropin, insulin-like growth factor-I and insulin on the proliferation of bovine granulosa cell in vitro, J. Endocrinol., 1993; 139: 67-75.
19. Spicer, L. J., Alpizar, E., and Echternkamp, S. E., Effects of insulin, insulin-like growth factor I, and gonadotropins on bovine granulosa cell proliferation, progesterone production, estradiol production, and (or) insulin-like growth factor I production in vitro, J. Anim. Sci., 1993; 71: 1232-1241.
20. Hill, D. J. and Milner, R. D. G., Insulin as a growth factor, Pediatr. Res., 1985; 19: 879-886.
21. Blachowski, S., Motyl T., Orzechowski, A., Grzelkowska, K., and Interrewicz, B., Comparison of metabolic effects of EGF, TGF-alpha and TGF-beta 1 in primary culture of fetal bovine myoblasts and rat L6 myoblasts, Int. J. Biochem., 1993; 25: 1571-1577.
22. Trippel, S. B., Wrobleski, J., Makoxer, A.M., Whelan, M. C., Schoenfeld, D., and Doctrow, S. R., Regulation of growth plate chondrocytes by insulin-like growth factor I and basic fibroblast growth factor, J. Bone Joint Surg. Am., 1993; 75: 177-189.
23. Nakashima, M., The effects of growth factors on DNA synthesis and alkaline phosphatase activity in bovine dental pulp cells, Cell Biol. Int. Rep., 1992; 16: 359-368.
24. Barinaga, M., Neurotrophic factors enter the clinic, Science, 1994; 264: 772-774.
25. Martinet, J. and Houdebine, L. M., Glande mammaire, mammogenese, facteurs de croissance, lactogenese. In: Martinet, J. and Houdebine, L. M., Eds., Biologie de la Lactation. INSERM/INRA, Paris, 1993; 59-72.
26. Oka, T., Yoshimura, M., Lavanderos, S., Wada, K., and Ohba, Y., Control of growth differentiation of the mammary gland by growth factors, J. Dairy Sci., 1991; 74: 2788-2800.
27. Plaut, K., Role of epidermal growth factor and transforming growth factors in mammary development and lactation, J. Dairy Sci., 1993; 76: 1526-1538.
28. Peri, I., Shamay, A., McGrath, M. F., Collier, R. J., and Gertler, A., Comparative mitogenic and galactopoietic effects of IGF-I, IGF-II and Des-3-IGF-I in bovine mammary gland in vitro, Cell Biol. Int. Rep., 1992; 16: 359-368.
29. 2-related polypeptide, from bovine milk, Eur. J. Biochem., 1991; 197: 353-358.
30. Berthon, P. and Salmon, H., Facteurs immunitaires des sécrétions mammaires. In: Martinet, J. and Houdebine, L. M., Eds., Biologie de la Lactation, INSERM/INRA, Paris, 1993; 389-414.
31. Klagsburn, M. and Neuman, J., The serum-free growth of Balb/C 3T3 cells in medium supplemented with bovine colostrum, J. Supramol. Struct., 1979; 11: 349-359.
32. Klagsburn, M., Bovine colostrum supports the serum free proliferation of epithelial cells but not of fibroblasts in long-term culture, J. Cell. Biol., 1980; 84: 808-814.
33. Ramirez, O. T., Sureshkumar, G. K., and Mutharasan, R., Bovine colostrum or milk as serum substitute for the cultivation of a mouse hybridoma, Biotechnol. Bioeng., 1990; 35: 882-889.
34. Pakkanen, R., Kantlinen, A., and Satama, L., Bovine colostrum as a serum substitute for the cultivation of mouse hybridomas, Appl. Microbiol. Biotechnol., 1992; 37: 451-456.
35. Pakkanen, R. and Neutra, M., Bovine colostrum ultrafiltrate; an effective supplement for the culture of mouse-mouse hybridoma cells, J. Immunol. Methods, 1994; 169: 63-71.
36. Pakkanen, R., Bovine colostrum ultrafiltrate supplemented with adult bovine serum and transferrin an effective FBS substitute for cultivation of vero and CHO K1 cells, In Vitro Cell. Dev. Biol., 1994; 30A: 295-299.
37. Steimer, K. S., Packard, R., Holden, D., and Klagsbrun, M., The serum-free growth of cultured cells in bovine colostrum and in milk obtained later in the lactation period, J. Cell. Physiol., 1981; 109: 223-234.
38. Steimer, K. and Klagsbrun, M., Serum-free growth of normal and transformed fibroblasts in milk: differential requirements for fibronectin, J. Cell. Biol., 1981; 88: 294-300.
39. Fassolitis, A. C., Novelli, R. M., and Larkin, E. P., Serum substitute in epithelial cell culture media: non-dry milk filtrate, Appl. Environ. Microbiol., 1981; 42: 200-203.
40. Sereni, A. and Basergha, R., Routine growth of cell lines in medium supplemented with milk instead of serum, Cell Biol. Int. Rep., 1981; 5: 339-345.
41. Aranda, P. L., Sanchez, L., Perez, M. D., and Calvo, M., Growth-promoting activity of bovine milk on a murine fibroblastic cell line and effect of heat treatment, Int. Dairy J., 1996; 6: 1-11.
42. Damerji, O., Derouiche, F., Legrand, C., Capiaumont, J., Bour, J. M., Maugras, M., Belleville, F., Nabet, P., Paquet, D., and Linden, G., Utilization of whey as a substitute for fetal calf serum in culture media, Biotechnol. Tech., 1988; 2: 253-258.
43. Derouiche, F., Legrand, C., Bour, J. M., Capiaumont, J., Gelot, M. A., Dousset, B., Belleville, F., Nabet, P., and Linden, G., Biochemical aspects of whey fractions capable of monitoring hybridoma proliferation: comparison with fetal calf serum, Lait, 1990; 70: 313-324.
44. Legrand, C., Capiaumont, J., Belleville, F., and Nabet, P., Comparison of metabolism of hybridoma cells cultured in media supplemented with whey or fetal calf serum, Biotechnol. Prog., 1993; 9: 573-579.
45. Capiaumont, J., Ostrovidov, S., Legrand, C., Belleville, F., and Nabet, P., Bovine whey substitute for FCS in CHO-K1 cell cultures, In Vitro Cell. Dev. Biol, 1996; 32: 8-12.
46. Fujiwara, S., Kadooka, Y., Hirota, T., and Nakazato, H., Screening for mitogenic activity of food microorganisms and their skim milk culture supernatants, J. Jpn. Soc. Nutr. Food Sci., 1990; 43: 203-208.
47. Guimont, C. and Badeche, C., Yoghurt serum for growth of cells: selective activity on hybridoma, In Vitro Cell. Dev. Biol., 1995; 31: 4-6.
48. Bourtourault, M., Buléon, R., Sampérez, S., and Jouan, P., Effet des protéines du lactosérum bovin sur la multiplication de cellules cancéreuses humaines, C.R. Soc. Biol., 1991; 185: 319-323.
49. Derouiche, F., Bour, J. M., Legrand, C., Capiaumont, J., Belleville, F., Linden, G., and Nabet, P., Improved long-term storage of hybridomas at -80°C using a bovine milk derivative, J. Immunol. Methods, 1989; 125: 13-18.
50. Pearlman, W. H., Hormones and tissue growth factor in milk: evolutionary implications, Endocr. Reg., 1991; 25: 4-9.
51. Fox, P. F. and Flynn, A., Biological properties of milk proteins. In: Fox, P. F., Ed., Advanced Dairy Chemistry-1: Proteins. Elsevier, New York, 1992; 255-284.
52. Schams, D., Growth factors in milk, Endrocr. Rev., 1994; 28: 3-8.
53. Janke, G. D. and Lazarus, L. H., A bombesin immunoreactive peptide in milk, Proc. Natl. Acad. Sci. U.S.A., 1984; 81: 578-582.
54. Hagemeister, H., Sick, H., and Barth, C. A., Nitrogen balance in the human and effects of milk constituents, IDF, 1990; 253:3-18.
55. Ollivier-Bousquet, M., Les hormones du lait: provenance et rôles, INRA Prod. Anim., 1993; 6: 253-263.
56. Murakami, H., Masui, H., Sato, G. H., Sueoka, N., Chow, T. P., and Kano-Sueoka, T., Growth of hybridoma cells in serum-free medium: ethanolamine is an essential component, Proc. Natl. Acad. Sci. U.S.A., 1982; 79: 1158-1162.
57. Cleveland, W. L., Wood, I., and Erlanger, B. F., Routine large-scale production of monoclonal antibodies on a protein free culture medium, J. Immunol. Methods, 1983; 56: 221-234.
58. Murakami, H., Serum-free media used for cultivation of hybridomas. In: Liss, A. R., Ed., Monoclonal Antibodies: Production and Application. 1989; 107-141.
59. Djiane, J., Daniel, N., Bignon, C., Paly, J., Waters, M., Vacher, P., and Dufy, B., Prolactin receptor and signal transduction to milk protein genes, Proc. Soc. Exp. Biol. Med., 1994; 206: 299-303.
60. Nabet, P., Belleville-Nabet, F., and Linden, G., Les peptides du lait ǎ activité physiologique. I. Facteurs de croissance dans le lait et le lactosérum, Lait, 1991; 71: 225-239.
61. Shing, Y. W. and Klagsbrun, M., Human and bovine milk contain different sets of growth factors, Endocrinology, 1984; 115: 273-282.
62. Campbell, P. G. and Baumrucker, C. R., Insulin-like growth factor I and its association with binding protein in bovine milk, J. Endocrinol., 1989; 120: 21-29.
63. Brown, K. D. and Blakely, D. M., Cell growth-promoting activity in mammary secretions of the goat, cow and sheep, Br. Vet. J., 1983; 139: 68-78.
64. Yagi, H., Suzuki, S., Noji, T., Nagashima, K., and Kurouma, T., Epidermal growth factor in cow's milk and milk formula, Acta Paediatr. Scand., 1986; 75: 233-235.
65. Rogers, M. L., Belford, D. A., Francis, G. L., and Ballard, F. J., Identification of fibroblast growth factors in bovine cheese whey, J. Dairy Res., 1995; 62: 501-507.
66. Yagi, H., Suzuki, S., Noji, T., Nagashima, K., and Kuroouma, T., Separation, purification and sequence identification of TGF-β1 and TGF-β2 from bovine milk, J. Protein Chem., 1991; 10: 565-575.
67. Growth Factor Reference Guide. ICM Biochemicals, Inc., 1995; 44-45.
68. Yamada, K., Ikeda, I., Sugahara, T., Sirhata, S., and Murakami, H., Screening of immunoglobulin production stimulating factor (IPSF) in foodstuffs using human-human hybridoma HB4C5 cells, Agric. Biol. Chem., 1989; 53: 2987-2991.
69. Nagaune, S., Azuma, N., Ishina, Y., Mori, H., Kaminogawa, S., and Yamauchi, K., DNA-synthesis stimulating peptide from bovine β-casein, Agric. Biol. Chem., 1989; 53: 3275-3278.
70. Konovalova, E. Y., Andreebva, I. V., and Prigoda, A. S., Design of serum-free nutrient media for culturing mammalian cells. III. Study of peptide spectrum of pancreatic casein hydrolysate and its ultrafiltration fractions with growth stimulating activity, Sov. Biotechnol, 1991; 5: 103-109.
71. Yamada, K., Nakajima, H., Ikeda, I., Shirahata, S., Enomoto, A., Kaminogawa, S., and Murakami, H., Animal cell culture and production of biologicals. In: Saski, R. and Ikura, K. J., Eds., Proceedings of the Third Annual Meeting of the Japanese Association of Animal Cell Technology, Kluwer, Dordrecht, 1991; 267-274.
72. Coste, M., Rochet, V., Léonil, J., Mollé, D., Bouchallab, and Tomé, D., Identification of C-terminal peptides of bovine β-casein that enhance proliferation of rat lymphocytes, Immunol. Lett., 1992; 33: 41-46.
73. MacDonald, R. S., Thornton, W. H., Jr., and Marshall, R. T., A cell culture to identify biologically active peptides generated by bacterial hydrolysis of casein, J. Dairy Sci., 1994; 77: 1167-1175.
74. Desmazeaud, M., Le lait milieu de culture, Microbiol. Alim. Nutr., 1990; 8: 313-325.
75. Otani, H., Monnai, M., and Hosono, A., Bovine κ-casein as inhibitor of the proliferation of mouse splenocytes induced by lipolysaccharide stimulation, Milchwissenschaft, 1992; 47: 512-515.
76. Otani, H. and Monnai, M., Inhibition of proliferative responses of mouse spleen lymphocytes by bovine milk κ-casein digests, Food Agric. Immunol, 1993; 5: 219-229.
77. Otani, H. and Hata, I., Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells by bovine milk caseins and their digests, J. Dairy Res., 1995; 62: 339-348.
78. Otani, H., Monnai, M., Kawasaki, Y., Kawakami, H., and Tanimoto, M., Inhibition of mitogen-induced proliferative responses of lymphocytes by bovine κ-casein glycopeptides having different carbohydrate chains, J. Dairy Res., 1995; 62: 349-357.
79. Polet, H. and Spieker-Polet, H., Mechanism of the growth-promoting effect of serum albumin on concanavalin A-activated lymphocytes: protective effects of the plasma proteins, J. Immunol., 1976; 117: 1275-1281.
80. Hemley, R., Kuhler, B. E., and Siviski, P., Absorption spectra for the complexes formed from vitamin A and β-lactoglobulin, Biophys. J., 1979; 28: 447-451.
81. Yoshida, S., Xiuyun, Y., and Nischiumi, T., The binding ability of α-lactalbumin and β-lactoglobulin to mutagenic heterocyclic amines, J. Dairy Sci., 1991; 74: 3741-3745.
82. Rejman, J. J., Oliver, S. P., Muenchen, R. A., and Turner, J. D., Proliferation of the MAC-T bovine mammary epithelial cell line in the presence of mammary secretion whey proteins, Cell Biol. Int. Rep., 1992; 16: 993-1001.
83. Moulti-Mati, F., Mati, A., Capiaumont, J., Belleville, F., Linden, G., and Nabet, P., Rôle de la β-lactoglobuline dans l'activité proliférative du lactoserum, Lait, 1991; 71: 543-553.
84. Mati, A., Moulti-Mati, F., Girardet, J. M., Fokou, E., Belleville-Nabet, F., Nabet, P., and Linden, G., Mitogenic activity of hydrophobic fractions of proteose peptone from cows, ewes and goats milk measured with MARK-3 hybridoma culture, J. Dairy Res., 1993; 60: 443-448.
85. Capiaumont, J., Legrand, C., Dousset, B., Parmentelot, I., Linden, G., Belleville, F., and Nabet, P., Whey and β-lactoglobulin: 2 milk byproducts that can replace fetal calf serum in mouse hybridoma cell culture, Lait, 1994; 74: 127-137.
86. Hashizuma, S., Kuroda, K., and Murakami, H., Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium, Biochem. Biophys. Acta, 1983; 763: 377-382.
87. Mincheva-Nilsson, L., Hammerstrôm, M. L., Juto, P., and Hammerstrôm, S., Human milk contains proteins that stimulate and suppress T lymphocyte proliferation, Clin. Exp. Immunol., 1990; 79: 463-469.
88. Machnicki, M., Biological properties of lactotransferrin, Folia Biol. (Praha), 1991; 37: 65-76.
89. Hambraeus, L. and Lonnerdal, B., The physiological role of lactoferrin, IDF, 1994; 97-107.
90. Byatt, J. C., Schuke, J. J., Comens, P. G., Johnson, D. A., and Collier, R. J., The effect of bovine lactoferrin on muscle growth in vivo and in vitro, Biochem. Biophys. Res. Commun., 1990; 173: 548-553.
91. Shinoda, I., Fukuwatari, Y., Shimamura, S., and Tomita, M., Stimulation by bovine lactoferrin of nerve growth factor synthesis/secretion in mouse LM cells, Biosci. Biotechnol. Biochem., 1993; 57: 890-893.
92. Oria, R., Iamail, M., Sanchez, L., Cavlo, M., and Brock, J., Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes, J. Dairy Res., 1993; 60: 363-369.
93. Torre, P. M. and Oliver, S. P., Inhibition of bovine peripheral mononuclear cell blastogenesis by fractional mammary secretion, Comp. Biochem. Physiol. B, 1989; 92: 157-165.
94. Rejman, J. J., Payne, K. D., Lewis, M. J., Torre, P. M., Muenchen, R. A., and Oliver, S. P., Identification of whey proteins that influence bovine blood mononuclear cell proliferation, J. Dairy. Sci., 1992; 75(Suppl.): 308.
95. Rejmann, J. J. and Oliver, S. P., Bimodal effects of lactoferrin on proliferation of an interleukin-2-dependent cytotoxic T-lymphocyte cell line, Food Agric. Immunol., 1993; 5: 123-128.
96. Xiuyun, Y. and Yoshida, S., Lactoperoxydase and lactoferrin; changes in post partum milk during bovine lactational disorders, Milchwissenschaft, 1995; 50: 67-70.
97. Parris, N., Purcell, J. M., and Ptashkin, S. M., Thermal denaturation of whey proteins in skim milk, J. Agric. Food Chem., 1991; 39: 2167-2171.
98. Morr, C. V. and Ha, E. Y. W., Whey protein concentrates and isolates: processing and functional properties, Crit. Rev. Food Sci. Nutr., 1993; 33: 431-476.
99. Jelen, P. and Rattray, W., Thermal denaturation of whey proteins. Heat-induced changes. IDF, 1995; 66-80.
100. Singh, H., Heat-induced changes in casein, including interactions with whey proteins, IDF, 1995; 86-99.
101. Singh, H., Creamer, L. K., and Newstead, D. F., Heat stability of concentrated milk, IDF, 1995; 12: 265-274.
102. O'Brien, J., Heat-induced changes in lactose: isomerization, degradation, Maillard browning, IDF, 1995; 134-162.
103. McCrae, C. H. and Muir, D. D., Heat stability of milk, IDF, 1995; 10: 206-230.
104. Jang, H. D. and Swaisgood, H. E., Disulfide bond formation between thermally denaturated β-lactoglobulin and κ-casein in casein micelles, J. Dairy Sci., 1990; 73: 900-905.
105. Sharma, S. K. and Dalgleish, D. G., Interactions between milk serum proteins and synthetic fat globule membrane during heating of homogenized whole milk, J. Agric. Food Chem., 1993; 41: 1407-1411.
106. Kim, H. H. Y. and Jimenez-Flores, R., Heat induced interactions between proteins of milk fat globule membrane and skim milk, J. Dairy Sci., 1995; 78:24-35.
107. Oria, R., Ismail, M., Sanchez, L., Calvo, M., and Brock, J. H., Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes, J. Dairy Res., 1993; 60: 363-369.
108. Puyol, P., Perez, M. D., Peiro, J. M., and Calvo, M., Effect of binding of retinol and palmitic acid to bovine β-lactoglobulin on its resistance to thermal denaturation, J. Dairy Sci., 1994; 77: 1494-1502.
109. Batt, C. A., Brady, J., and Sawyer, L., Design improvements of β-lactoglobulin, Trends Food Sci. Technol., 1994; 5: 261-265.
110. Pellegrino, L., Tirelli, A, and Masotti, F., Evidence of whey protein glycosylation occurring in dried milk. In: IDF, Ed., 24th International Dairy Congress, ANCIDF, Brussels, 1994; 115116.
111. Shida, K., Takamizawa, K., Nagaoka, M., Kushiro, A., and Osawa, T., Enterotoxin-binding glycoproteins in a proteose peptone fraction of heated bovine milk, J. Dairy Sci., 1994; 77: 930-939.
112. Neichev, Kh., Ivanovska, N., Shirova, L., Slavcheva, E., Stoyonova, P., Georgiev, D., Abrashev, I., Velcheva, P., and Yanchev, I., Immunomodulating properties of a glycomacropeptide isolated from whey. Activation of macrophages and polymorphonuclear leukocytes, Acta Microbiol. Bull., 1990; 26: 19-25.
113. Shinoda, T., Hayase, F., and Kato, H., Suppression of cell-cycle progression during the S-phase of rat fibroblasts by 3-deoxyglucosone, a Maillard reaction intermediate, Biosci. Biotechnol. Biochem., 1994; 58: 2215-2219.
114. Vardri, A., Biological roles of oligosaccharides: all of the theories are correct, Glycobiology, 1993; 3: 97-130.
115. Reinerdes, E. H., New aspects of naturally occurring proteases in bovine milk, J. Dairy Sci., 1983; 66: 1591-1600.
116. Fox, P. F., Indigenous enzymes in milk: proteinases. In: Fox, P. F., Ed., Advanced Dairy Chemistry-1: Proteins. Elsevier, New York, 1992; 310-321.
117. Teuber, M., Production of chymosin by microorganisms and its use for cheese making, IDF, 1990; 251: 3-15.
118. Baer, A. and Collin, J. C., Determination of residual activity of milk-clotting enzymes in cheese, IDF, 1993; 284: 18-22.
119. Schmidt, J. L., Tourneur, C., and Lenoir, J., Fonctions et choix des bactéries lactiques en technologies laitiěres. In: De Roissart, H. and Luquet, F. M., Eds., Bactéries Lactiques, II. Lorica, 1994; 37-45.
120. Mietton, B., Weber, F., Desmazeaud, M., and De Roissart, H., Transformation du lait en fromage. In: De Roissart, H. and Luquet, F. M., Eds., Bacteries Lactiques, II. Lorica, 1994; 55-133.
121. Visser, S., Proteolytic enzymes and their action on milk proteins. A review, Neth. Milk Dairy J., 1981; 35: 65-88.
122. Monnet, V. and Gripon, J. C., Métabolisme azoté des bactéries lactiques. In: De Roissart, H. and Luquet, F. M., Eds. Bactéries Lactiques, I. Lorica, 1994; 331-347.
123. Fiat, A. M. and Jolles, P., Caseins of various origins and biologically active casein peptides and oligosaccharides: structural and physiological aspects, Mol. Cell. Biochem., 1989; 87: 5-30.
124. Meisel, H. and Schlimme, E., Milk proteins: precursors of bioactive peptides, Trends Food Sci. Technol., 1990; 1: 41-45.
125. Maubois, J. L. and Leonil, J., Peptides du laitǎactivité biologique, Lait, 1989; 69: 245-269.
126. Schlimme, E. and Meisel, H., Biological peptides derived from milk proteins. Structural, physiological and analytical aspects, Nahrung, 1995; 39: 1-20.
127. Motion, R. L., Hydrolysates of milk proteins, Proc. Nutr. Soc. N.Z., 1992; 17: 56-63.
128. Julius M., Janusz, M., and Lisowski, J., A colostral protein that induces the growth and differentiation of resting B lymphocytes, J. Immunol., 1988; 140: 1366-1371.
129. Pike, S. E., Markey, S. P., and James, C. L., The role of lactic acid in autocrine B-cell stimulation, Proc. Natl. Acad. Sci. U.S.A., 1991; 88: 11081-11085.
130. Brown, M. E., Interactions of β-lactoglobulin and α-lactalbumin with lipids: a review, J. Dairy Sci., 1984; 67: 713-722.
131. Diaz de Villegas, M. C., Oria, R., Sala, F. J., and Calvo, M., Lipid binding by β-lactoglobulin of cow milk, Milchwissenschaft, 1987; 42: 357-358.
132. Rask, L., Anundi, H., and Peterson, P. A., The primary structure of the human retinol-binding protein, Fed. Eur. Biol. Soc. Lett., 1979; 104: 55-58.
133. Fugate, R. D. and Song, P. S., Spectroscopic characterization of β-lactoglobulin-retinol complex, Biochim. Biophys. Acta, 1980; 625: 28-42.
134. Godovac-Zimmermann, J. and Braunitzer, G., Modern aspects of the primary structure and function of β-lactoglobulin, Milchwissenschaft, 1987; 42: 294-297.
135. Godovac-Zimmermann, J., The structural motif of β-lactoglobulin and retinol-binding protein: a basic framework for binding and transport of small hydrophobic molecules, Trends Biochem. Sci., 1988; 13: 64-67.
136. Alais, C., Les protides. La caséine et le phenomène de la coagulation. In: Sepaic, Ed. Science du Lait: Principe de Techniques Laitiěres. Paris, 1984; 184-186.
137. Pessen, H., Purcell, J. M., and Farell, H. M., Proton relaxation rates of water in dilute solutions of β-lactoglobulin. Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of a self-associating globular protein, Biochim. Biophys. Acta, 1985; 828: 1-12.
138. Berridge, M. J., Inositol triphosphate and diacylglycerol: two interacting second messengers, Annu. Rev. Biochem., 1987; 56: 159-193.
139. Woodlock, T. J., Segel, G. B., and Lightman, M. A., Diacylglycerol and calcium induce rapid enhancement of a system amino acid transport by independent mechanisms in human T lymphocytes, J. Cell Physiol., 1989; 141: 33-39.
140. Baumy, J. J. and Brule, G., Binding of bivalent cations to α-lactalbumin and β-lactoglobulin: effect of pH and ionic strength, Lait, 1988; 68: 33-48.
141. Van Deal, P. and Deelstra, H., Speciation of selenium in bovine whey, Soc. Chem., 1989; 72: 112-115.
142. McKeehan, W. L., Hamilton, W. G., and Ham, R. G., Selenium is an essential trace nutrient for growth of WI-38 diploid human fibroblasts, Proc. Natl. Acad. Sci. U.S.A., 1976; 73: 2023-2027.
143. Takahashi, T., Kaminogawa, S., Kuwata, T., Ando, O., and Yamauchi, K., T cell recognition of β-lactoglobulin, Agric. Biol. Chem., 1988; 52: 2485-2491.
144. Said, H. M., Ong, D. E., and Shingleton, J. L., Intestinal uptake of retinol: enhancement by bovine milk β-lactoglobulin. Am., J. Clin. Nutr., 1989; 49: 690-694.
145. Brown, E. M., Carroll, R. J., Pfeffer, P. E., and Sampugna, J., Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidyl-choline, Lipids, 1983; 18: 111-114.
146. Haddad, Z. H., Faca, M. D., Vinkalra, M. S., and Sanjiv Verma, M. D., IgE: antibodies digests of beta lactoglobulin: significance in food hypersensitivity, Ann. Allergy, 1979; 42: 368-371.
147. Malik, Z., Bottomtey, R., and Austen, B., Allergenic properties of the genetic variants A and B of bovine β-lactoglobulin, Int. Arch. Allergy Appl. Immunol., 1988; 86: 245-248.
148. Malik, Z., Bottomtey, R., and Austen, B., Allergenic properties of the genetic variants of bovine β-lactoglobulin, Biochem. Soc. Trans., 1988; 16: 338-340.
149. Otani, H., Antigenically reactive regions of bovine milk proteins, Jpn. Agric. Res. Q., 1989; 22: 135-142.
150. Otani, H. and Tokita, F., Contribution of the sugar moiety in the browning product between β-lactoglobulin and lactose as an antigenic determinant, Jpn. J. Zootechnol. Sci., 1982; 53; 344-350.
151. Otani, H., Monta, S. I., and Tokita, F., Studies on the antigenicity of the browning product between β-lactoglobulin and lactose, Jpn. J. Zootechnol. Sci., 1985; 56: 67-74.
152. Otani, H., Morita, S. I., and Tokita, Studies on the antigenicity of the browning product between β-lactoglobulin and lactose: antigenic activities of peptides 25-61 and 62-107, Jpn. J. Zootechnol. Sci., 1985; 56: 341-346.
153. Otani, H., Morita, S. I., and Tokita, Studies on the antigenicity of the browning product between β-lactoglobulin and lactose: antigenic activities of peptides obtained by the cleavage at arginin peptide bonds in regions 25-107 and 108-145, Jpn. J. Zootechnol. Sci., 1985; 56: 987-993.
154. Otani, H., Ulhio, T., and Tokita, F., Antigenic reactivities of chemically modifies β-lactoglobulin with antiserum to bovine β-lactoglobulin, Agric. Biol. Chem., 1985; 49: 2531-2536.
155. Otani, H. and Hosono, A., Location of antigenic sites in a browning product between β-lactoglobulin and lactose, Jpn. J. Zootechnol. Sci., 1987; 58: 474-482.
156. Otani, H., Morita, S. I., and Tokita, F., Antigenic reactivity of S-carboxymethylated β-lactoglobulin with antiserum to β-lactoglobulin from UHT processed milk, Jpn. J. Zootechnol. Sci., 1984; 55: 287-289.
157. Otani, H. and Hosono, A., Antigenic reactive regions of S-carboxymethylated β-lactoglobulin, Agric. Biol. Chem., 1987; 51: 531-536.
158. Kaminogawa, S., Shimizu, M., Ametani, A., Hattori, M., Ando, O., Hachimura, S., Nakamura, Y., Totsuka, M., and Yamauchi, K., Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin, Biochim. Biophys. Acta, 1989; 998: 50-56.
159. Tsuji, N., Kurisaki, J., Mizumachi, K., and Kaminogawa, S., Localization of T-cell determinants on bovine β-lactoglobulin, Immunol. Lett., 1993; 37: 215-221.
160. Girardet, J. M. and Linden, G., PP3 component of bovine milk: a phosphorylated whey glycoprotein, J. Dairy Res., 1996, 63: 333-350.
161. Kanno, C., Purification and separation of multiple forms of lactophorin from bovine milk whey and their immunological and electrophoretic properties, J. Dairy Sci., 1989; 72: 883-891.
162. Sørensen, E. S. and Petersen, T. E., Phosphorylation, glycosylation and amino acid sequence of component PP3 from the proteose-peptone fraction of bovine milk, J. Dairy Res., 1993; 60: 535-542.
163. Johnsen, L. B., Sørensen, E. S., Petersen, T. E., and Berglund, L., Characterization of a bovine mammary gland cDNA reveals homology with a mouse and rat immune protein GlyCAM-1, Biochim. Biophys. Acta, 1995; 1260: 116-118.
164. Groenen, M. A. M., Dijkhof, R. J. M., and van der Poel, J. J., Characterization of a GlyCAM/-like gene (glycosylation-dependent cell adhesion molecule 1) which is highly and specifically expressed in the lactating bovine mammary gland, Gene, 1995; 158; 189-195.
165. Girardet, J. M., Coddeville, B., Planke, Y., Strecker, G., Campagna, S., Spik, G., and Linden, G., Structure of glycopeptides isolated from bovine milk component PP3, Eur. J. Biochem., 1995; 234; 939-946.
166. Sato, T., Furukawa, K., Greenwalt, D. E., and Kobata, A., Most bovine milk fat globule membrane glycoproteins contain asparagine-linked sugar chains with GalNAcβ1-4GlcNAc groups, J. Biochem., 1993; 114: 890-900.
167. Nakata, N., Furukawa, K., Greenwalt, D. E., Sato, T., and Kobata, A., Structural study of the sugar chains of CD36 purified from bovine mammary epithelial cells: occurrence of novel hybrid-type sugar chains containing the NeuAcα2-6GalNacβ1-4GlcNAc and the Manα1-2Manα1-3Manα1-6Man groups, Biochemistry, 1993; 32: 4369-4383.
168. Sato, T., Takio, K., Kobata, A., Greenwalt, D. E., and Furukawa, K., Site-specific glycosylation of bovine butyrophilin, J. Biochem., 1995; 117: 147-157.
169. Dowbenko, D., Andalibi, A., Young, P. E., Lusis, A., and Lasky, L. A., Structure and chromosomal localization of the murine gene encoding GLYCAM 1. A mucin-like endothelial ligand for L-selectin, J. Biol. Chem., 1993; 268: 4525-4529.
170. Imai, Y., Lasky, L. A., and Rosen, S. D., Sulphatation requirement for GlyCAM-1, an endothelial ligand for L-selectin, Nature (London), 1993; 361: 555-557.
171. Hemmerich, S., Bertozzi, C. R., Leffler, H., and Rosen, S. D., Identification of the sulfated monosaccharides of GlyCAM-1, an endothelial-derived ligand for L-selectin, Biochemistry, 1994; 33: 4820-4829.
172. Hemmerich, S. and Rosen, S. D., 6′-Sulfated sialyl Lewis x is a major capping group of GlyCAM-1, Biochemistry, 1994; 33: 4830-4835.
173. Lasky, L. A., Singer, M. S., Dowbenko, D., Imai, Y., Henzel, W. J., Grimley, C., Fennie, C., Gillet, N., Watson, S. R., and Rosen, An endothelial ligand for L-selectin is a novel mucin-like molecule, Cell, 1992; 69: 927-938.
174. Montreuil, J., Spatial conformation of glycans and glycoproteins, Biol Cell, 1984; 51: 115-132.
175. Le Meste, M., Colas, B., Blond, G., and Simatos, D., Influence of glycosylation on the hydration properties of caseinates, J. Dairy Res., 1989; 56: 479-486.
176. Guimont, C., personal communication.