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Volumn 20, Issue 9, 2010, Pages 609-629

Equine milk proteins: Chemistry, structure and nutritional significance

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGOLOGY; BOVINE MILK; COWS' MILK; CROSS-REACTIVITY; FUNCTIONAL PROPERTIES; HUMAN MILK; HUMAN NUTRITION; MILK PROTEIN; PROTEIN COMPOSITION; PROTEIN CONTENTS; THERAPEUTIC PROPERTIES; WHEY PROTEINS;

EID: 77954834274     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2010.02.007     Document Type: Review
Times cited : (172)

References (266)
  • 2
    • 0000370077 scopus 로고
    • Susceptibility of buffalo and cow κ-caseins to chymosin action
    • Addeo F., Martin P., Ribadeau-Dumas B. Susceptibility of buffalo and cow κ-caseins to chymosin action. Milchwissenschaft 1984, 39:202-205.
    • (1984) Milchwissenschaft , vol.39 , pp. 202-205
    • Addeo, F.1    Martin, P.2    Ribadeau-Dumas, B.3
  • 6
    • 0000433381 scopus 로고
    • Nitrogenous components of milk. Non protein nitrogen fractions of human milk
    • Academic Press, San Diego, CA, USA, R.G. Jensen (Ed.)
    • Atkinson S.A., Lönnerdal B. Nitrogenous components of milk. Non protein nitrogen fractions of human milk. Handbook of milk composition 1995, 369-387. Academic Press, San Diego, CA, USA. R.G. Jensen (Ed.).
    • (1995) Handbook of milk composition , pp. 369-387
    • Atkinson, S.A.1    Lönnerdal, B.2
  • 7
    • 0001777028 scopus 로고
    • Non-protein nitrogen components in human milk: biochemistry and potential roles
    • CRC Press, Boca Raton, FL, USA, S.A. Atkinson, B. Lönnerdal (Eds.)
    • Atkinson S.A., Schnurr C., Donovan S.M., Lönnerdal B. Non-protein nitrogen components in human milk: biochemistry and potential roles. Protein and non-protein nitrogen in human milk 1989, 117-136. CRC Press, Boca Raton, FL, USA. S.A. Atkinson, B. Lönnerdal (Eds.).
    • (1989) Protein and non-protein nitrogen in human milk , pp. 117-136
    • Atkinson, S.A.1    Schnurr, C.2    Donovan, S.M.3    Lönnerdal, B.4
  • 9
    • 24944504306 scopus 로고    scopus 로고
    • Biological effects of milk proteins and their peptides with emphasis on those related to the gastrointestinal ecosystem
    • Baldi A., Politis I., Pecorini C., Fusi E., Roubini C., Dell'Orto V. Biological effects of milk proteins and their peptides with emphasis on those related to the gastrointestinal ecosystem. Journal of Dairy Research 2005, 72:66-72.
    • (2005) Journal of Dairy Research , vol.72 , pp. 66-72
    • Baldi, A.1    Politis, I.2    Pecorini, C.3    Fusi, E.4    Roubini, C.5    Dell'Orto, V.6
  • 11
    • 0019347114 scopus 로고
    • Bovine alpha-lactalbumin C and alpha S1-, beta- and kappa-caseins of Bali (Banteng) cattle, Bos (Bibos) javanicus
    • Bell K., Hopper K.E., McKenzie H.A. Bovine alpha-lactalbumin C and alpha S1-, beta- and kappa-caseins of Bali (Banteng) cattle, Bos (Bibos) javanicus. Australian Journal of Biological Sciences 1981, 34:149-159.
    • (1981) Australian Journal of Biological Sciences , vol.34 , pp. 149-159
    • Bell, K.1    Hopper, K.E.2    McKenzie, H.A.3
  • 15
    • 84886191702 scopus 로고
    • International Dairy Federation, Brussels
    • Berlin P.J. Kumiss. Annual bulletin, IV 1962, International Dairy Federation, Brussels, pp. 4-16.
    • (1962) Kumiss. Annual bulletin, IV , pp. 4-16
    • Berlin, P.J.1
  • 19
    • 77954834318 scopus 로고
    • L'ingestion chez la jument. Etude de quelques facteurs de variation au tours du cycle gestation-lactation. Implications, nutritionelles et métaboliques. Thése Doct. Ing., ENSA Rennes, Univ. Rennes I, France
    • Boulot, S. (1987). L'ingestion chez la jument. Etude de quelques facteurs de variation au tours du cycle gestation-lactation. Implications, nutritionelles et métaboliques. Thése Doct. Ing., ENSA Rennes, Univ. Rennes I, France.
    • (1987)
    • Boulot, S.1
  • 20
    • 10044268957 scopus 로고    scopus 로고
    • α-Lactalbumin
    • Kluwer Academic/Plenum Publishers, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • Brew K. α-Lactalbumin. Proteins 2003, Vol. 1:387-419. Kluwer Academic/Plenum Publishers, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 387-419
    • Brew, K.1
  • 21
    • 0010519790 scopus 로고    scopus 로고
    • Lactoferrin structure - function relationships
    • Humana Press, Totowa, NJ, USA, T.W. Hutchens, B. Lönnerdal (Eds.)
    • Brock J.H. Lactoferrin structure - function relationships. Lactoferrin: Interactions and biological functions 1997, 3-38. Humana Press, Totowa, NJ, USA. T.W. Hutchens, B. Lönnerdal (Eds.).
    • (1997) Lactoferrin: Interactions and biological functions , pp. 3-38
    • Brock, J.H.1
  • 22
    • 0034490342 scopus 로고    scopus 로고
    • Biological activities of bovine macropeptide
    • Brody E.P. Biological activities of bovine macropeptide. British Journal of Nutrition 2000, 84:S39-S46.
    • (2000) British Journal of Nutrition , vol.84
    • Brody, E.P.1
  • 23
    • 0001257050 scopus 로고
    • Verrgleichende Untersuchungen zur Struktur und Grobe von Casein Micellen in der Milchverschiedener Species
    • Buchheim W., Lund S., Scholtissek J. Verrgleichende Untersuchungen zur Struktur und Grobe von Casein Micellen in der Milchverschiedener Species. Kieler Milchwirtschaffliche Forschungsberichte 1989, 41:253-265.
    • (1989) Kieler Milchwirtschaffliche Forschungsberichte , vol.41 , pp. 253-265
    • Buchheim, W.1    Lund, S.2    Scholtissek, J.3
  • 25
    • 0027298687 scopus 로고
    • Food allergy in childhood. Hypersensitivity to cows' milk allergens
    • Businco L. Food allergy in childhood. Hypersensitivity to cows' milk allergens. Clinical and Experimental Allergy 1993, 23:481-483.
    • (1993) Clinical and Experimental Allergy , vol.23 , pp. 481-483
    • Businco, L.1
  • 28
    • 0037409126 scopus 로고    scopus 로고
    • Nitrogeneous components of human milk: non-protein nitrogen, true protein and free amino acids
    • Carratù B., Boniglia C., Scalise F., Ambruzzi A.M., Sanzini E. Nitrogeneous components of human milk: non-protein nitrogen, true protein and free amino acids. Food Chemistry 2003, 81:357-362.
    • (2003) Food Chemistry , vol.81 , pp. 357-362
    • Carratù, B.1    Boniglia, C.2    Scalise, F.3    Ambruzzi, A.M.4    Sanzini, E.5
  • 32
    • 33748449287 scopus 로고    scopus 로고
    • Bioactivity of β-lactoglobulin and α-lactalbumin - technological implications for processing
    • Chatterton D.E.W., Smithers G., Roupas P., Brodkorb A. Bioactivity of β-lactoglobulin and α-lactalbumin - technological implications for processing. International Dairy Journal 2006, 16:1229-1240.
    • (2006) International Dairy Journal , vol.16 , pp. 1229-1240
    • Chatterton, D.E.W.1    Smithers, G.2    Roupas, P.3    Brodkorb, A.4
  • 33
    • 28844490606 scopus 로고    scopus 로고
    • Use of donkey's milk for a fermented beverage with lactobacilli
    • Chiavari C., Coloretti F., Nanni M., Sorrentino E., Grazia L. Use of donkey's milk for a fermented beverage with lactobacilli. Lait 2005, 85:481-490.
    • (2005) Lait , vol.85 , pp. 481-490
    • Chiavari, C.1    Coloretti, F.2    Nanni, M.3    Sorrentino, E.4    Grazia, L.5
  • 35
    • 3543062840 scopus 로고    scopus 로고
    • Protein dissection experiments reveal key differences in the equilibrium folding of α-lactalbumin and the calcium binding lysozymes
    • Chowdhury F.A., Fairman R., Bi Y., Rigotti D.J., Raleigh D.P. Protein dissection experiments reveal key differences in the equilibrium folding of α-lactalbumin and the calcium binding lysozymes. Biochemistry 2004, 43:9961-9967.
    • (2004) Biochemistry , vol.43 , pp. 9961-9967
    • Chowdhury, F.A.1    Fairman, R.2    Bi, Y.3    Rigotti, D.J.4    Raleigh, D.P.5
  • 37
    • 33846523391 scopus 로고    scopus 로고
    • Mare's milk: monitoring the effect of thermal treatments on whey proteins stability by SDS capillary electrophoresis (CE-SDS)
    • Civardi G., Curadi M.C., Orlandi M., Cattaneo T.M.P., Giangiacomo R. Mare's milk: monitoring the effect of thermal treatments on whey proteins stability by SDS capillary electrophoresis (CE-SDS). Milchwissenschaft 2007, 62:32-35.
    • (2007) Milchwissenschaft , vol.62 , pp. 32-35
    • Civardi, G.1    Curadi, M.C.2    Orlandi, M.3    Cattaneo, T.M.P.4    Giangiacomo, R.5
  • 38
    • 0033822081 scopus 로고    scopus 로고
    • s1-casein, milk composition and coagulation properties of goat milk
    • s1-casein, milk composition and coagulation properties of goat milk. Small Ruminant Research 2000, 38:123-134.
    • (2000) Small Ruminant Research , vol.38 , pp. 123-134
    • Clark, S.1    Sherbon, J.W.2
  • 41
    • 0000186040 scopus 로고
    • Composition of mare's colostrum and milk. Fat content, fatty acid composition and vitamin content
    • Csapó J., Stefler J., Martin T.G., Makray S., Csapó-Kiss Zs Composition of mare's colostrum and milk. Fat content, fatty acid composition and vitamin content. International Dairy Journal 1995, 5:393-402.
    • (1995) International Dairy Journal , vol.5 , pp. 393-402
    • Csapó, J.1    Stefler, J.2    Martin, T.G.3    Makray, S.4    Csapó-Kiss, Z.5
  • 42
    • 0001587942 scopus 로고
    • Composition of mare's colostrum and milk. Protein content, amino acid composition and contents of macro- and micro-elements
    • Csapó-Kiss Zs., Stefler J., Martin T.G., Makray S., Csapó J. Composition of mare's colostrum and milk. Protein content, amino acid composition and contents of macro- and micro-elements. International Dairy Journal 1995, 5:403-415.
    • (1995) International Dairy Journal , vol.5 , pp. 403-415
    • Csapó-Kiss, Z.1    Stefler, J.2    Martin, T.G.3    Makray, S.4    Csapó, J.5
  • 44
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Kluwer Academic/Plenum Publishers, New York, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • De Kruif C.G., Holt C. Casein micelle structure, functions and interactions. Proteins 2003, Vol. 1:233-276. Kluwer Academic/Plenum Publishers, New York, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 233-276
    • De Kruif, C.G.1    Holt, C.2
  • 46
    • 0026948222 scopus 로고
    • Nonprotein nitrogen and protein distribution in the milk of cows
    • De Peters E.J., Ferguson J.D. Nonprotein nitrogen and protein distribution in the milk of cows. Journal of Dairy Science 1992, 75:3192-3209.
    • (1992) Journal of Dairy Science , vol.75 , pp. 3192-3209
    • De Peters, E.J.1    Ferguson, J.D.2
  • 50
    • 0012157531 scopus 로고
    • Le lait de jument et sa production: particularités et facteurs de variation
    • Doreau M. Le lait de jument et sa production: particularités et facteurs de variation. Lait 1994, 74:401-418.
    • (1994) Lait , vol.74 , pp. 401-418
    • Doreau, M.1
  • 51
    • 0025515917 scopus 로고
    • Yield and composition of milk from lactating mares: effect of lactation stage and individual differences
    • Doreau M., Boulet S., Bartlet J.-P., Patureau-Mirand P. Yield and composition of milk from lactating mares: effect of lactation stage and individual differences. Journal of Dairy Research 1990, 57:449-454.
    • (1990) Journal of Dairy Research , vol.57 , pp. 449-454
    • Doreau, M.1    Boulet, S.2    Bartlet, J.-P.3    Patureau-Mirand, P.4
  • 52
    • 0001150472 scopus 로고
    • Recent knowledge on mare milk production: a review
    • Doreau M., Boulot S. Recent knowledge on mare milk production: a review. Livestock Production Science 1989, 22:213-235.
    • (1989) Livestock Production Science , vol.22 , pp. 213-235
    • Doreau, M.1    Boulot, S.2
  • 54
    • 2642531859 scopus 로고    scopus 로고
    • Dairy animals: horse
    • Academic Press, London, UK, H. Roginski, J.A. Fuquay, P.F. Fox (Eds.)
    • Doreau M., Martin-Rosset W. Dairy animals: horse. Encyclopedia of dairy sciences 2002, 630-637. Academic Press, London, UK. H. Roginski, J.A. Fuquay, P.F. Fox (Eds.).
    • (2002) Encyclopedia of dairy sciences , pp. 630-637
    • Doreau, M.1    Martin-Rosset, W.2
  • 55
    • 41149094954 scopus 로고    scopus 로고
    • Food proteins as precursors of bioactive peptides: classification into families
    • Dziuba M., Darewicz M. Food proteins as precursors of bioactive peptides: classification into families. Food Science and Technology International 2007, 13:393-404.
    • (2007) Food Science and Technology International , vol.13 , pp. 393-404
    • Dziuba, M.1    Darewicz, M.2
  • 56
    • 0030288545 scopus 로고    scopus 로고
    • Influence of glycosylation on micelle-stabilizing ability and biological properties of C-terminal fragments of cow's κ-casein
    • Dziuba J., Minkiewicz P. Influence of glycosylation on micelle-stabilizing ability and biological properties of C-terminal fragments of cow's κ-casein. International Dairy Journal 1996, 6:1017-1044.
    • (1996) International Dairy Journal , vol.6 , pp. 1017-1044
    • Dziuba, J.1    Minkiewicz, P.2
  • 57
    • 2642700187 scopus 로고
    • Soy protein allergy
    • Raven Press, New York, NY, USA, R.N. Hamburger (Ed.) Food intolerance in infancy: Allergology, immunology, and gastroenterology
    • Eastman E.J. Soy protein allergy. Carnation nutrition education series 1989, Vol. 1:223-236. Raven Press, New York, NY, USA. R.N. Hamburger (Ed.).
    • (1989) Carnation nutrition education series , vol.1 , pp. 223-236
    • Eastman, E.J.1
  • 61
    • 33846850537 scopus 로고    scopus 로고
    • The challenge of cow milk protein allergy
    • El-Agamy E.I. The challenge of cow milk protein allergy. Small Ruminant Research 2007, 68:64-72.
    • (2007) Small Ruminant Research , vol.68 , pp. 64-72
    • El-Agamy, E.I.1
  • 62
    • 77954834875 scopus 로고    scopus 로고
    • A comparative study of milk proteins from different species. II. Electrophoretic patterns, molecular characterization, amino acid composition and immunological relationships. A comparative study of milk proteins from different species. II. Electrophoretic patterns, molecular characterization, amino acid composition and immunological relationships. In Third Alexandria Conference on Food Science and Technology, Alexandria, Egypt.
    • El-Agamy, E. I., Abou-Shloue, Z. I., & Abdel-Kader, Y. I. (1997). A comparative study of milk proteins from different species. II. Electrophoretic patterns, molecular characterization, amino acid composition and immunological relationships. A comparative study of milk proteins from different species. II. Electrophoretic patterns, molecular characterization, amino acid composition and immunological relationships. In Third Alexandria Conference on Food Science and Technology (pp. 51-62), Alexandria, Egypt.
    • (1997) , pp. 51-62
    • El-Agamy, E.I.1    Abou-Shloue, Z.I.2    Abdel-Kader, Y.I.3
  • 63
    • 0030455418 scopus 로고    scopus 로고
    • Purification and characterization of lactoferrin, lactoperoxidase, lysozyme and immunoglobulins from camel's milk
    • El-Agamy E.I., Ruppanner R., Ismail A., Champagne C.P., Assaf R. Purification and characterization of lactoferrin, lactoperoxidase, lysozyme and immunoglobulins from camel's milk. International Dairy Journal 1996, 6:129-145.
    • (1996) International Dairy Journal , vol.6 , pp. 129-145
    • El-Agamy, E.I.1    Ruppanner, R.2    Ismail, A.3    Champagne, C.P.4    Assaf, R.5
  • 64
    • 0036762489 scopus 로고    scopus 로고
    • The effect of mare's milk consumption on functional elements of phagocytosis of human neutrophils granulocytes from healthy volunteers
    • Ellinger S., Linscheid K.P., Jahnecke S., Goerlich R., Endbergs H. The effect of mare's milk consumption on functional elements of phagocytosis of human neutrophils granulocytes from healthy volunteers. Food and Agricultural Immunology 2002, 14:191-200.
    • (2002) Food and Agricultural Immunology , vol.14 , pp. 191-200
    • Ellinger, S.1    Linscheid, K.P.2    Jahnecke, S.3    Goerlich, R.4    Endbergs, H.5
  • 65
    • 0026095436 scopus 로고
    • Killing of gram-negative bacteria by lactoferrin and lysozyme
    • Ellison R.T., Giehl T.J. Killing of gram-negative bacteria by lactoferrin and lysozyme. Journal of Clinical Investigation 1991, 88:1080-1091.
    • (1991) Journal of Clinical Investigation , vol.88 , pp. 1080-1091
    • Ellison, R.T.1    Giehl, T.J.2
  • 66
    • 8844240048 scopus 로고    scopus 로고
    • Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin. Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis
    • El-Zahar K., Sitohy M., Choiset Y., Métro F., Haertlé T., Chobert J.-M. Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin. Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis. International Dairy Journal 2005, 15:17-27.
    • (2005) International Dairy Journal , vol.15 , pp. 17-27
    • El-Zahar, K.1    Sitohy, M.2    Choiset, Y.3    Métro, F.4    Haertlé, T.5    Chobert, J.-M.6
  • 67
    • 0030697202 scopus 로고    scopus 로고
    • Properties of human milk and their relationship with maternal nutrition
    • Emmett P.M., Rogers I.S. Properties of human milk and their relationship with maternal nutrition. Early Human Development 1997, 49:S7-S28.
    • (1997) Early Human Development , vol.49
    • Emmett, P.M.1    Rogers, I.S.2
  • 68
    • 77954834172 scopus 로고    scopus 로고
    • ExPASy ProtParam Tool, Swiss Institute of Bioinfomatics. Retrieved 16.10.09 from
    • ExPASy ProtParam Tool, Swiss Institute of Bioinfomatics. (2009). Retrieved 16.10.09 from http://www.expasy.org/tools/pi_tool.html.
    • (2009)
  • 69
    • 0031864664 scopus 로고    scopus 로고
    • Allergy to mare's milk
    • Fanta C., Ebner C. Allergy to mare's milk. Allergy 1998, 53:539-540.
    • (1998) Allergy , vol.53 , pp. 539-540
    • Fanta, C.1    Ebner, C.2
  • 73
    • 44549088735 scopus 로고    scopus 로고
    • The casein micelle: historical aspects, current concepts and significance
    • Fox P.F., Brodkorb A. The casein micelle: historical aspects, current concepts and significance. International Dairy Journal 2008, 18:677-684.
    • (2008) International Dairy Journal , vol.18 , pp. 677-684
    • Fox, P.F.1    Brodkorb, A.2
  • 75
    • 77954834763 scopus 로고
    • Über Säuglingsernährung mit Stutenmilch - erste Mitteilung
    • Freudenberg V.E. Über Säuglingsernährung mit Stutenmilch - erste Mitteilung. Annales Paediatrici 1948, 171:338-364.
    • (1948) Annales Paediatrici , vol.171 , pp. 338-364
    • Freudenberg, V.E.1
  • 76
    • 84957849017 scopus 로고
    • Über Säuglingsernährung mit Stutenmilch - zweite Mitteilung
    • Freudenberg V.E. Über Säuglingsernährung mit Stutenmilch - zweite Mitteilung. Annales Paediatrici 1948, 171:49-64.
    • (1948) Annales Paediatrici , vol.171 , pp. 49-64
    • Freudenberg, V.E.1
  • 77
    • 77954834478 scopus 로고
    • Aportacion preliminar a la composicion del calostro en yeguas de pura raza Española (Andaluza) y las modificaciones que experimenta en su transito a leche
    • Fuentes-García F., Abascal C.G., del Castillo Caracuel A., Quiles Sotillo A., Vinuesa Silva M. Aportacion preliminar a la composicion del calostro en yeguas de pura raza Española (Andaluza) y las modificaciones que experimenta en su transito a leche. Archivos de Zootecnia 1991, 40:153-160.
    • (1991) Archivos de Zootecnia , vol.40 , pp. 153-160
    • Fuentes-García, F.1    Abascal, C.G.2    del Castillo Caracuel, A.3    Quiles Sotillo, A.4    Vinuesa Silva, M.5
  • 79
    • 8544237958 scopus 로고
    • Hypersensitivity of human subjects to bovine milk proteins: a review
    • Ghosh J., Malhotra G.S., Mathur B.N. Hypersensitivity of human subjects to bovine milk proteins: a review. Indian Journal of Dairy Science 1989, 42:744-749.
    • (1989) Indian Journal of Dairy Science , vol.42 , pp. 744-749
    • Ghosh, J.1    Malhotra, G.S.2    Mathur, B.N.3
  • 81
    • 33745683584 scopus 로고    scopus 로고
    • Determination of the phosphorylation level and deamidation susceptibility of equine β-casein
    • 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.
    • (2006) Proteomics , vol.6 , pp. 3707-3717
    • Girardet, J.-M.1    Miclo, L.2    Florent, S.3    Mollé, D.4    Gaillard, J.-L.5
  • 83
    • 0021880659 scopus 로고
    • The amino-acid sequence of β-lactoglobulin II from horse colostrum (Equus caballus, Perissodactyla): β-lactoglobulins are retinol-binding proteins
    • Godovac-Zimmerman J., Conti A., Liberatori J., Braunitzer G. The amino-acid sequence of β-lactoglobulin II from horse colostrum (Equus caballus, Perissodactyla): β-lactoglobulins are retinol-binding proteins. Biological Chemistry Hoppe-Seyler 1985, 366:601-608.
    • (1985) Biological Chemistry Hoppe-Seyler , vol.366 , pp. 601-608
    • Godovac-Zimmerman, J.1    Conti, A.2    Liberatori, J.3    Braunitzer, G.4
  • 84
    • 0023319880 scopus 로고
    • Identification and the primary structure of equine α-lactalbumin B and C (Equus caballus, Perissodactyla
    • Godovac Zimmerman J., Shaw D., Conti A., McKenzie H. Identification and the primary structure of equine α-lactalbumin B and C (Equus caballus, Perissodactyla. Biological Chemistry Hoppe-Seyler 1987, 368:427-433.
    • (1987) Biological Chemistry Hoppe-Seyler , vol.368 , pp. 427-433
    • Godovac Zimmerman, J.1    Shaw, D.2    Conti, A.3    McKenzie, H.4
  • 86
    • 0018165282 scopus 로고
    • Lactoferrin is a marker for prolactin response in mouse mammary explants
    • Green M.R., Pastewka J.V. Lactoferrin is a marker for prolactin response in mouse mammary explants. Endocrinology 1978, 103:1510-1513.
    • (1978) Endocrinology , vol.103 , pp. 1510-1513
    • Green, M.R.1    Pastewka, J.V.2
  • 87
    • 35748976232 scopus 로고    scopus 로고
    • Composition, physicochemical properties, nitrogen fraction distribution, and amino acid profile of donkey milk
    • Guo H.Y., Pang K., Zhang X.Y., Zhao L., Chen S.W., Dong M.L., et al. Composition, physicochemical properties, nitrogen fraction distribution, and amino acid profile of donkey milk. Journal of Dairy Science 2007, 90:1635-1643.
    • (2007) Journal of Dairy Science , vol.90 , pp. 1635-1643
    • Guo, H.Y.1    Pang, K.2    Zhang, X.Y.3    Zhao, L.4    Chen, S.W.5    Dong, M.L.6
  • 88
    • 0025979995 scopus 로고
    • The complete amino acid sequence of feline β-lactoglobulin II and a partial revision of the equine β-lactoglobulin II sequence
    • Halliday J.A., Bell K., Shaw D.C. The complete amino acid sequence of feline β-lactoglobulin II and a partial revision of the equine β-lactoglobulin II sequence. Biochimica et Biophysica Acta 1991, 1077:25-30.
    • (1991) Biochimica et Biophysica Acta , vol.1077 , pp. 25-30
    • Halliday, J.A.1    Bell, K.2    Shaw, D.C.3
  • 89
    • 0343681424 scopus 로고
    • Nutritional aspects of milk proteins
    • Applied Science Publishers, London, UK, P.F. Fox (Ed.) Developments in dairy chemistry
    • Hambræus L. Nutritional aspects of milk proteins. Proteins 1982, Vol. 1:289-313. Applied Science Publishers, London, UK. P.F. Fox (Ed.).
    • (1982) Proteins , vol.1 , pp. 289-313
    • Hambræus, L.1
  • 91
    • 19544372654 scopus 로고    scopus 로고
    • Nutritional aspects of milk proteins
    • Kluwer Academic/Plenum Publishers, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • Hambræus L., Lönnerdal B. Nutritional aspects of milk proteins. Proteins 2003, Vol. 1:605-645. Kluwer Academic/Plenum Publishers, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 605-645
    • Hambræus, L.1    Lönnerdal, B.2
  • 92
    • 58149132303 scopus 로고    scopus 로고
    • Biofunctional properties of bioactive peptides of milk origin
    • Haque H., Chand R., Kapila S. Biofunctional properties of bioactive peptides of milk origin. Food Reviews International 2009, 25:28-43.
    • (2009) Food Reviews International , vol.25 , pp. 28-43
    • Haque, H.1    Chand, R.2    Kapila, S.3
  • 93
    • 0028813886 scopus 로고
    • Structure of human diferric lactoferrin refined at 2.2 Å resolution
    • Haridas M., Anderson B.F., Baker E.N. Structure of human diferric lactoferrin refined at 2.2 Å resolution. Acta Crystallographica D 1995, 51:629-646.
    • (1995) Acta Crystallographica D , vol.51 , pp. 629-646
    • Haridas, M.1    Anderson, B.F.2    Baker, E.N.3
  • 94
    • 13244277961 scopus 로고    scopus 로고
    • Preparation of antioxidant enzymatic hydrolyzates from α-lactalbumin and β-lactoglobulin. Identification of peptides by HPLC-MS/MS
    • Hernández-Ledesma B., Dávalos A., Bartolomé B., Amigo L. Preparation of antioxidant enzymatic hydrolyzates from α-lactalbumin and β-lactoglobulin. Identification of peptides by HPLC-MS/MS. Journal of Agricultural and Food Chemistry 2005, 53:588-593.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 588-593
    • Hernández-Ledesma, B.1    Dávalos, A.2    Bartolomé, B.3    Amigo, L.4
  • 95
    • 49749143329 scopus 로고    scopus 로고
    • β-Lactoglobulin as a source of bioactive peptides
    • Hernández-Ledesma B., Recio I., Amigo L. β-Lactoglobulin as a source of bioactive peptides. Amino Acids 2008, 35:257-265.
    • (2008) Amino Acids , vol.35 , pp. 257-265
    • Hernández-Ledesma, B.1    Recio, I.2    Amigo, L.3
  • 96
    • 0013889060 scopus 로고
    • On the conformation of caseins. Optical rotatory properties
    • Herskovitis T.T. On the conformation of caseins. Optical rotatory properties. Biochemistry 1966, 5:1018-1026.
    • (1966) Biochemistry , vol.5 , pp. 1018-1026
    • Herskovitis, T.T.1
  • 97
    • 0028143689 scopus 로고
    • Cow milk allergy within the spectrum of atopic disorders
    • Hill D.J. Cow milk allergy within the spectrum of atopic disorders. Clinical and Experimental Allergy 1994, 24:1137-1143.
    • (1994) Clinical and Experimental Allergy , vol.24 , pp. 1137-1143
    • Hill, D.J.1
  • 98
    • 0033504365 scopus 로고    scopus 로고
    • The natural history of intolerance to soy and extensively hydrolysed formula in infants with multiple food protein intolerance
    • Hill D.J., Heine R.G., Cameron D.J.S., Francis D.E.M., Bines J.E. The natural history of intolerance to soy and extensively hydrolysed formula in infants with multiple food protein intolerance. Journal of Pediatrics 1999, 135:118-121.
    • (1999) Journal of Pediatrics , vol.135 , pp. 118-121
    • Hill, D.J.1    Heine, R.G.2    Cameron, D.J.S.3    Francis, D.E.M.4    Bines, J.E.5
  • 100
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: evolution of the concept and its implications for dairy technology
    • 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.
    • (1996) Netherlands Milk and Dairy Journal , vol.50 , pp. 85-111
    • Holt, C.1    Horne, D.S.2
  • 101
    • 0021294881 scopus 로고
    • Interrelationships of constituents and partition of salts in milk samples from eight species
    • A
    • Holt C., Jenness R. Interrelationships of constituents and partition of salts in milk samples from eight species. Comparative Biochemistry and Physiology 1984, 77A:175-282.
    • (1984) Comparative Biochemistry and Physiology , vol.77 , pp. 175-282
    • Holt, C.1    Jenness, R.2
  • 103
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: casting light on the black boxes, the structure in dairy products
    • Horne D.S. Casein interactions: casting light on the black boxes, the structure in dairy products. International Dairy Journal 1998, 8:171-177.
    • (1998) International Dairy Journal , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 105
    • 0023753752 scopus 로고
    • A prospective study of cow's milk allergy in exclusively breast-fed infants. Incidence, pathogenetic role of early inadvertent exposure to cow's milk formula, and characterization of bovine milk protein in human milk
    • Høst A. A prospective study of cow's milk allergy in exclusively breast-fed infants. Incidence, pathogenetic role of early inadvertent exposure to cow's milk formula, and characterization of bovine milk protein in human milk. Acta Paediatrica Scandinavica 1988, 77:663-670.
    • (1988) Acta Paediatrica Scandinavica , vol.77 , pp. 663-670
    • Høst, A.1
  • 106
    • 0025863510 scopus 로고
    • Importance of the first meal on the development of cow's milk allergy and intolerance
    • Høst A. Importance of the first meal on the development of cow's milk allergy and intolerance. Allergy Proceedings 1991, 12:227-232.
    • (1991) Allergy Proceedings , vol.12 , pp. 227-232
    • Høst, A.1
  • 107
    • 0347973687 scopus 로고    scopus 로고
    • Immunoglobulins in mammary secretions
    • Kluwer Academic/Plenum Publishers, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • Hurley W.L. Immunoglobulins in mammary secretions. Proteins 2003, Vol. 1:422-447. Kluwer Academic/Plenum Publishers, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 422-447
    • Hurley, W.L.1
  • 111
    • 77954834883 scopus 로고    scopus 로고
    • Lactose malabsorption
    • Kluwer Academic/Plenum Publishers, New York, NY, USA, P.L.H. McSweeney, P.F. Fox (Eds.) Advanced dairy chemistry
    • Ingram C.J.E., Swallow D.M. Lactose malabsorption. Lactose, water, salts and minor constituents 2003, Vol. 3:203-229. Kluwer Academic/Plenum Publishers, New York, NY, USA. 3rd ed. P.L.H. McSweeney, P.F. Fox (Eds.).
    • (2003) Lactose, water, salts and minor constituents , vol.3 , pp. 203-229
    • Ingram, C.J.E.1    Swallow, D.M.2
  • 112
    • 0018133389 scopus 로고
    • Cow's milk as a cause of infantile colic in breast-fed infants
    • Jakobsson I., Lindberg T. Cow's milk as a cause of infantile colic in breast-fed infants. Lancet 1978, 11:437-446.
    • (1978) Lancet , vol.11 , pp. 437-446
    • Jakobsson, I.1    Lindberg, T.2
  • 115
    • 0012159691 scopus 로고
    • Comparison of structures of micellar caseins of milk of cows, goats and mares with human milk casein
    • Jasińska B., Jaworska G. Comparison of structures of micellar caseins of milk of cows, goats and mares with human milk casein. Animal Science Papers and Reports 1991, 7:45-55.
    • (1991) Animal Science Papers and Reports , vol.7 , pp. 45-55
    • Jasińska, B.1    Jaworska, G.2
  • 116
    • 0016517114 scopus 로고
    • Heat stability and reactivation of mare milk lysozyme
    • Jauregui-Adell J. Heat stability and reactivation of mare milk lysozyme. Journal of Dairy Science 1975, 58:835-838.
    • (1975) Journal of Dairy Science , vol.58 , pp. 835-838
    • Jauregui-Adell, J.1
  • 117
    • 36749050495 scopus 로고    scopus 로고
    • Evolutionary distance from human homologs reflects allergenicity of animal food proteins
    • Jenkins J.A., Breiteneder H., Mills C. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. Journal of Allergy and Clinical Immunology 2007, 120:1399-1405.
    • (2007) Journal of Allergy and Clinical Immunology , vol.120 , pp. 1399-1405
    • Jenkins, J.A.1    Breiteneder, H.2    Mills, C.3
  • 119
    • 0002620750 scopus 로고
    • The composition of milk
    • Academic Press, New York, NY, USA, B.L. Larson, V.R. Smith (Eds.)
    • Jenness R. The composition of milk. Lactation: A comprehensive treatise 1974, Vol. III:3-107. Academic Press, New York, NY, USA. B.L. Larson, V.R. Smith (Eds.).
    • (1974) Lactation: A comprehensive treatise , vol.3 , pp. 3-107
    • Jenness, R.1
  • 120
    • 0000055359 scopus 로고
    • The composition of milk of various species: a review
    • Jenness R., Sloan R.E. The composition of milk of various species: a review. Dairy Science Abstracts 1970, 32:599-612.
    • (1970) Dairy Science Abstracts , vol.32 , pp. 599-612
    • Jenness, R.1    Sloan, R.E.2
  • 122
  • 124
    • 0019343242 scopus 로고
    • Presence of O-glycosidic linkage through serine residue in κ-casein component from bovine mature milk
    • 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 1981, 27:231-241.
    • (1981) Journal of Nutritional Science and Vitaminology , vol.27 , pp. 231-241
    • Kanamori, M.1    Doi, H.2    Ideno, S.3    Ibuki, F.4
  • 125
    • 84886155869 scopus 로고
    • Traditional fermented milk of the world
    • Elsevier Applied Science Publisher, London, UK, Y. Nakazawa, A. Hosono (Eds.)
    • Kanbe M. Traditional fermented milk of the world. Functions of fermented milk: Challenges for the health sciences 1992, Elsevier Applied Science Publisher, London, UK. Y. Nakazawa, A. Hosono (Eds.).
    • (1992) Functions of fermented milk: Challenges for the health sciences
    • Kanbe, M.1
  • 128
    • 0035711472 scopus 로고    scopus 로고
    • Energetics of three-state unfolding of a protein: canine milk lysozyme
    • Koshiba T., Kobashigawa Y., Demura M., Nitta K. Energetics of three-state unfolding of a protein: canine milk lysozyme. Protein Engineering 2001, 14:967-974.
    • (2001) Protein Engineering , vol.14 , pp. 967-974
    • Koshiba, T.1    Kobashigawa, Y.2    Demura, M.3    Nitta, K.4
  • 129
    • 0034724253 scopus 로고    scopus 로고
    • Structure and thermodynamics of the extraordinary stable molten globule state of canine milk lysozyme
    • Koshiba T., Yao M., Kobashigawa Y., Demura M., Nakagawa A., Tanaka I., et al. Structure and thermodynamics of the extraordinary stable molten globule state of canine milk lysozyme. Biochemistry 2000, 39:3248-3257.
    • (2000) Biochemistry , vol.39 , pp. 3248-3257
    • Koshiba, T.1    Yao, M.2    Kobashigawa, Y.3    Demura, M.4    Nakagawa, A.5    Tanaka, I.6
  • 130
    • 0016957163 scopus 로고
    • Isolation of κ-casein-like proteins from milk of various species
    • Kotts C., Jenness R. Isolation of κ-casein-like proteins from milk of various species. Journal of Dairy Science 1976, 59:816-822.
    • (1976) Journal of Dairy Science , vol.59 , pp. 816-822
    • Kotts, C.1    Jenness, R.2
  • 131
    • 77954834083 scopus 로고
    • Kouevodstvo i konnyl Sport 35(4), 27; cited from Dairy Science Abstracts (1965)
    • Kudryaslov, A., & Krylova, O. (1965). Kouevodstvo i konnyl Sport 35(4), 27; cited from Dairy Science Abstracts (1965), 28, 2299.
    • (1965) , vol.28-2299
    • Kudryaslov, A.1    Krylova, O.2
  • 132
    • 0346210620 scopus 로고
    • The composition of mare's milk in three horse breeds with reference to N-acetylneuraminic acid
    • Kulisa M. The composition of mare's milk in three horse breeds with reference to N-acetylneuraminic acid. Acta Agraria et Silvestria. Series Zootechnica 1977, 27:25-37.
    • (1977) Acta Agraria et Silvestria. Series Zootechnica , vol.27 , pp. 25-37
    • Kulisa, M.1
  • 135
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 1982, 157:105-132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 136
    • 20844440532 scopus 로고    scopus 로고
    • The balance between caseins and whey proteins in cow's milk determines its allergenicity
    • Lara-Villoslada F., Olivares M., Xaus J. The balance between caseins and whey proteins in cow's milk determines its allergenicity. Journal of Dairy Science 2005, 88:1654-1660.
    • (2005) Journal of Dairy Science , vol.88 , pp. 1654-1660
    • Lara-Villoslada, F.1    Olivares, M.2    Xaus, J.3
  • 137
    • 0018463012 scopus 로고
    • Biosynthesis and secretion of milk proteins: a review
    • Larson B.L. Biosynthesis and secretion of milk proteins: a review. Journal of Dairy Research 1979, 46:161-174.
    • (1979) Journal of Dairy Research , vol.46 , pp. 161-174
    • Larson, B.L.1
  • 138
    • 0032846808 scopus 로고    scopus 로고
    • Elucidation of the antistaphylococcal action of lactoferrin and lysozyme
    • Leitch E.C., Willcox M.D.P. Elucidation of the antistaphylococcal action of lactoferrin and lysozyme. Journal of Medical Microbiology 1999, 48:867-871.
    • (1999) Journal of Medical Microbiology , vol.48 , pp. 867-871
    • Leitch, E.C.1    Willcox, M.D.P.2
  • 140
    • 0031843536 scopus 로고    scopus 로고
    • Immunonutrition: the pediatric experience
    • Levy J. Immunonutrition: the pediatric experience. Nutrition 1998, 14:641-647.
    • (1998) Nutrition , vol.14 , pp. 641-647
    • Levy, J.1
  • 142
    • 84913000732 scopus 로고
    • The composition of mare's milk
    • Linton R.G. The composition of mare's milk. Journal of Dairy Research 1937, 8:143-172.
    • (1937) Journal of Dairy Research , vol.8 , pp. 143-172
    • Linton, R.G.1
  • 143
    • 0012705286 scopus 로고    scopus 로고
    • Fermented milk
    • Elsevier, London, UK, R. Robinson, C. Batt, P. Patel (Eds.)
    • Litopoulou-Tzanetaki E., Tzanetakis N. Fermented milk. Encyclopedia of food microbiology 2000, Vol. 2:774-805. Elsevier, London, UK. R. Robinson, C. Batt, P. Patel (Eds.).
    • (2000) Encyclopedia of food microbiology , vol.2 , pp. 774-805
    • Litopoulou-Tzanetaki, E.1    Tzanetakis, N.2
  • 144
    • 0037483715 scopus 로고    scopus 로고
    • Lactoferrin
    • Kluwer Academic/Plenum Publishers, New York, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • Lönnerdal B. Lactoferrin. Proteins 2003, Vol. 1:449-460. Kluwer Academic/Plenum Publishers, New York, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 449-460
    • Lönnerdal, B.1
  • 145
    • 0002694040 scopus 로고
    • Medical uses of whole and fermented mare milk in Russia
    • Lozovich S. Medical uses of whole and fermented mare milk in Russia. Cultured Dairy Products Journal 1995, 30:18-21.
    • (1995) Cultured Dairy Products Journal , vol.30 , pp. 18-21
    • Lozovich, S.1
  • 146
    • 0026904789 scopus 로고
    • Effect of calcium on the stability of mares' milk lysozyme
    • Lyster R.L.J. Effect of calcium on the stability of mares' milk lysozyme. Journal of Dairy Research 1992, 59:331-338.
    • (1992) Journal of Dairy Research , vol.59 , pp. 331-338
    • Lyster, R.L.J.1
  • 148
    • 0036916729 scopus 로고    scopus 로고
    • Protein and fat composition of mare's milk: some nutritional remarks with reference to human and cow's milk
    • Malacarne M., Martuzzi F., Summer A., Mariani P. Protein and fat composition of mare's milk: some nutritional remarks with reference to human and cow's milk. International Dairy Journal 2002, 12:869-897.
    • (2002) International Dairy Journal , vol.12 , pp. 869-897
    • Malacarne, M.1    Martuzzi, F.2    Summer, A.3    Mariani, P.4
  • 151
    • 0000504993 scopus 로고    scopus 로고
    • Chemical composition and nutritional properties of commercial products of mare milk powder
    • Marconi E., Panfili G. Chemical composition and nutritional properties of commercial products of mare milk powder. Journal of Food Composition and Analysis 1998, 11:178-187.
    • (1998) Journal of Food Composition and Analysis , vol.11 , pp. 178-187
    • Marconi, E.1    Panfili, G.2
  • 152
    • 0012192858 scopus 로고
    • Composition and physico-chemical properties of lactating mare's milk: variation of the nitrogeneous and mineral constituents during lactation
    • Mariani P., Martuzzi F., Catalano A.L. Composition and physico-chemical properties of lactating mare's milk: variation of the nitrogeneous and mineral constituents during lactation. Annali Della Facolta Di Parma 1993, 13:43-58.
    • (1993) Annali Della Facolta Di Parma , vol.13 , pp. 43-58
    • Mariani, P.1    Martuzzi, F.2    Catalano, A.L.3
  • 153
    • 0035735227 scopus 로고    scopus 로고
    • Physicochemical properties, gross composition, energy value and nitrogen fractions of Halflinger nursing mare milk throughout 6 lactation months
    • Mariani P., Summer A., Martuzzi F., Formaggioni P., Sabbioni A., Catalano A.L. Physicochemical properties, gross composition, energy value and nitrogen fractions of Halflinger nursing mare milk throughout 6 lactation months. Animal Research 2001, 50:415-425.
    • (2001) Animal Research , vol.50 , pp. 415-425
    • Mariani, P.1    Summer, A.2    Martuzzi, F.3    Formaggioni, P.4    Sabbioni, A.5    Catalano, A.L.6
  • 154
    • 0000723082 scopus 로고    scopus 로고
    • s1-casein is expressed in human mammary epithelial cells during lactation
    • s1-casein is expressed in human mammary epithelial cells during lactation. Lait 1996, 76:523-535.
    • (1996) Lait , vol.76 , pp. 523-535
    • Martin, P.1    Brignon, G.2    Furet, J.P.3    Leroux, C.4
  • 155
    • 77954834095 scopus 로고    scopus 로고
    • Mare milk composition: recent findings about protein fractions and mineral content
    • Wageningen Academic Publishers, Wageningen, The Netherlands, N. Margilia, W. Martin-Rosset (Eds.)
    • Martuzzi F., Doreau M. Mare milk composition: recent findings about protein fractions and mineral content. Nutrition and feeding of the broodmare - EAAP publication No. 20 2006, 65-76. Wageningen Academic Publishers, Wageningen, The Netherlands. N. Margilia, W. Martin-Rosset (Eds.).
    • (2006) Nutrition and feeding of the broodmare - EAAP publication No. 20 , pp. 65-76
    • Martuzzi, F.1    Doreau, M.2
  • 157
    • 67649221525 scopus 로고    scopus 로고
    • Two-dimensional cartography of equine β-casein variants achieved by isolation of phosphorylation isoforms and control of the deamidation phenomenon
    • Matéos A., Girardet J.-M., Mollé D., Dary A., Miclo L., Gaillard J.-L. Two-dimensional cartography of equine β-casein variants achieved by isolation of phosphorylation isoforms and control of the deamidation phenomenon. Journal of Dairy Science 2009, 92:2389-2399.
    • (2009) Journal of Dairy Science , vol.92 , pp. 2389-2399
    • Matéos, A.1    Girardet, J.-M.2    Mollé, D.3    Dary, A.4    Miclo, L.5    Gaillard, J.-L.6
  • 158
    • 68949201518 scopus 로고    scopus 로고
    • Equine as1-casein: characterization of alternative splicing isoforms and determination of phosphorylation levels
    • Matéos A., Miclo L., Mollé D., Dary A., Girardet J.-M., Gaillard J.-L. Equine as1-casein: characterization of alternative splicing isoforms and determination of phosphorylation levels. Journal of Dairy Science 2009, 92:3604-3615.
    • (2009) Journal of Dairy Science , vol.92 , pp. 3604-3615
    • Matéos, A.1    Miclo, L.2    Mollé, D.3    Dary, A.4    Girardet, J.-M.5    Gaillard, J.-L.6
  • 159
    • 0017049350 scopus 로고
    • Comparative study of the amino acid sequences of the caseinomacropeptides from seven species
    • Mercier J.-C., Chobert J.-M., Addeo F. Comparative study of the amino acid sequences of the caseinomacropeptides from seven species. FEBS Letters 1976, 72:208-214.
    • (1976) FEBS Letters , vol.72 , pp. 208-214
    • Mercier, J.-C.1    Chobert, J.-M.2    Addeo, F.3
  • 160
    • 51449093529 scopus 로고    scopus 로고
    • Factors influencing nutritional and health profile of milk and milk products
    • Michaelidou A.M. Factors influencing nutritional and health profile of milk and milk products. Small Ruminant Research 2008, 79:42-50.
    • (2008) Small Ruminant Research , vol.79 , pp. 42-50
    • Michaelidou, A.M.1
  • 161
    • 34248140193 scopus 로고    scopus 로고
    • The primary structure of a low-Mr multiphosphorylated variant of β-casein in equine milk
    • Miclo L., Girardet J.-M., Egito A.S., Mollé D., Martin P., Gaillard J.-L. The primary structure of a low-Mr multiphosphorylated variant of β-casein in equine milk. Proteomics 2007, 7:1327-1335.
    • (2007) Proteomics , vol.7 , pp. 1327-1335
    • Miclo, L.1    Girardet, J.-M.2    Egito, A.S.3    Mollé, D.4    Martin, P.5    Gaillard, J.-L.6
  • 163
    • 3543112680 scopus 로고    scopus 로고
    • Proteomic tools to characterize the protein fraction of Equidae milk
    • Miranda G., Mahé M.-F., Leroux C., Martin P. Proteomic tools to characterize the protein fraction of Equidae milk. Proteomics 2004, 4:2496-2509.
    • (2004) Proteomics , vol.4 , pp. 2496-2509
    • Miranda, G.1    Mahé, M.-F.2    Leroux, C.3    Martin, P.4
  • 164
    • 0030179121 scopus 로고    scopus 로고
    • Elevation of lactoferrin gene expression in developing, ductal, resting, and regressing parenchymal epithelium of the ruminant mammary gland
    • Molenaar A.J., Kuys Y.M., Davis S.R., Wilkins R.J., Mead P.E., Tweedie J.W. Elevation of lactoferrin gene expression in developing, ductal, resting, and regressing parenchymal epithelium of the ruminant mammary gland. Journal of Dairy Science 1996, 79:1198-1208.
    • (1996) Journal of Dairy Science , vol.79 , pp. 1198-1208
    • Molenaar, A.J.1    Kuys, Y.M.2    Davis, S.R.3    Wilkins, R.J.4    Mead, P.E.5    Tweedie, J.W.6
  • 165
    • 0031875136 scopus 로고    scopus 로고
    • Microparticle-enhanced nephelometric immunoassay of lysozyme in milk and other human body fluids
    • Montagne P., Cuillière M.L., Molé C., Béné M.C., Faure G. Microparticle-enhanced nephelometric immunoassay of lysozyme in milk and other human body fluids. Clinical Chemistry 1998, 44:1610-1615.
    • (1998) Clinical Chemistry , vol.44 , pp. 1610-1615
    • Montagne, P.1    Cuillière, M.L.2    Molé, C.3    Béné, M.C.4    Faure, G.5
  • 167
    • 34247105337 scopus 로고    scopus 로고
    • Efficacy of donkey's milk in treating highly problematic cow's milk allergic children: an in vivo and in vitro study
    • Monti G., Bertino M., Muratore M.C., Coscia A., Cresi F., Silvestro L., et al. Efficacy of donkey's milk in treating highly problematic cow's milk allergic children: an in vivo and in vitro study. Pediatric Allergy and Immunology 2007, 18:258-264.
    • (2007) Pediatric Allergy and Immunology , vol.18 , pp. 258-264
    • Monti, G.1    Bertino, M.2    Muratore, M.C.3    Coscia, A.4    Cresi, F.5    Silvestro, L.6
  • 169
    • 34249666246 scopus 로고    scopus 로고
    • Equine-lysozyme: the molecular basis of folding, self-assembly and innate amyloid toxicity
    • Morozova-Roche L. Equine-lysozyme: the molecular basis of folding, self-assembly and innate amyloid toxicity. FEBS Letters 2007, 581:2587-2592.
    • (2007) FEBS Letters , vol.581 , pp. 2587-2592
    • Morozova-Roche, L.1
  • 170
    • 0029937138 scopus 로고    scopus 로고
    • Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity
    • Mullally M.M., Meisel H., Fitzgerald R.J. Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity. Biological Chemistry Hoppe-Seyler 1996, 377:259-260.
    • (1996) Biological Chemistry Hoppe-Seyler , vol.377 , pp. 259-260
    • Mullally, M.M.1    Meisel, H.2    Fitzgerald, R.J.3
  • 171
  • 172
    • 0021740940 scopus 로고
    • Expression of κ-casein in normal and neoplastic rat mammary gland is under the control of prolactin
    • Nakhasi H.L., Grantham F.H., Gullino P.M. Expression of κ-casein in normal and neoplastic rat mammary gland is under the control of prolactin. Journal of Biological Chemistry 1984, 259:14894-14898.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 14894-14898
    • Nakhasi, H.L.1    Grantham, F.H.2    Gullino, P.M.3
  • 174
    • 0012160430 scopus 로고
    • Milchleistung und Milchzusammenstzung von Studen im Verlauf der Laktation
    • 119-129
    • Neseni R., Flade R., Heidler G., Steger H. Milchleistung und Milchzusammenstzung von Studen im Verlauf der Laktation. Archiv Tierzucht 1958, 1. 119-129.
    • (1958) Archiv Tierzucht , vol.1
    • Neseni, R.1    Flade, R.2    Heidler, G.3    Steger, H.4
  • 176
    • 69249215154 scopus 로고    scopus 로고
    • Introduction: alpha-lactalbumin, a multifunctional protein that specifies lactose synthesis in the Golgi
    • Neville M.C. Introduction: alpha-lactalbumin, a multifunctional protein that specifies lactose synthesis in the Golgi. Journal of Mammary Gland Biology and Neoplasia 2009, 14:211-212.
    • (2009) Journal of Mammary Gland Biology and Neoplasia , vol.14 , pp. 211-212
    • Neville, M.C.1
  • 177
    • 0005436026 scopus 로고
    • The physical properties of human and bovine milk
    • Academic Press, San Diego, CA, US, R.G. Jensen (Ed.)
    • Neville M.C., Jensen R.G. The physical properties of human and bovine milk. Handbook of milk composition 1995, 81-85. Academic Press, San Diego, CA, US. R.G. Jensen (Ed.).
    • (1995) Handbook of milk composition , pp. 81-85
    • Neville, M.C.1    Jensen, R.G.2
  • 178
    • 0023642591 scopus 로고
    • The calcium-binding properties of equine lysozyme
    • Nitta K., Tsuge H., Sugai S., Shimazaki K. The calcium-binding properties of equine lysozyme. FEBS Letters 1987, 223:405-408.
    • (1987) FEBS Letters , vol.223 , pp. 405-408
    • Nitta, K.1    Tsuge, H.2    Sugai, S.3    Shimazaki, K.4
  • 179
    • 44949222558 scopus 로고    scopus 로고
    • Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions
    • Nonaka Y., Aizawa T., Akieda D., Yasui M., Watanabe M., Watanabe N., et al. Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions. Proteins 2008, 72:313-322.
    • (2008) Proteins , vol.72 , pp. 313-322
    • Nonaka, Y.1    Aizawa, T.2    Akieda, D.3    Yasui, M.4    Watanabe, M.5    Watanabe, N.6
  • 181
    • 0742331980 scopus 로고    scopus 로고
    • Heat-induced coagulation of milk
    • Kluwer Academic/Plenum Publishers, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • O'Connell J.E., Fox P.F. Heat-induced coagulation of milk. Proteins 2003, Vol. 1:879-945. Kluwer Academic/Plenum Publishers, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 879-945
    • O'Connell, J.E.1    Fox, P.F.2
  • 182
    • 1842850220 scopus 로고
    • Milk composition and formula selection for hand-rearing young animals
    • First annual Dr. Scholl nutrition conference on the nutrition of captive wild animals, Lincoln Park Zoological Gardens, Chicago, Illinois, USA, E.R. Maschgan, M.E. Allen, L.E. Fisher (Eds.)
    • Oftedal O.T. Milk composition and formula selection for hand-rearing young animals. The nutrition of captive wild animals 1980, 67-83. First annual Dr. Scholl nutrition conference on the nutrition of captive wild animals, Lincoln Park Zoological Gardens, Chicago, Illinois, USA. E.R. Maschgan, M.E. Allen, L.E. Fisher (Eds.).
    • (1980) The nutrition of captive wild animals , pp. 67-83
    • Oftedal, O.T.1
  • 183
    • 0020841751 scopus 로고
    • Lactation in the horse: milk composition and intake by foals
    • Oftedal O.T., Hintz H.F., Schryver H.F. Lactation in the horse: milk composition and intake by foals. Journal of Nutrition 1983, 113:2096-2106.
    • (1983) Journal of Nutrition , vol.113 , pp. 2096-2106
    • Oftedal, O.T.1    Hintz, H.F.2    Schryver, H.F.3
  • 184
    • 0023959080 scopus 로고
    • Interspecies variation in milk composition among horses, zebras and asses (Perissodactyla: Equidae)
    • Oftedal O.T., Jenness R. Interspecies variation in milk composition among horses, zebras and asses (Perissodactyla: Equidae). Journal of Dairy Research 1988, 55:57-66.
    • (1988) Journal of Dairy Research , vol.55 , pp. 57-66
    • Oftedal, O.T.1    Jenness, R.2
  • 185
    • 0002000556 scopus 로고
    • Subunit components of casein micelles from bovine, ovine, caprine and equine milk
    • Ono T., Kohno H., Odagiri S., Takagi T. Subunit components of casein micelles from bovine, ovine, caprine and equine milk. Journal of Dairy Research 1989, 56:61-68.
    • (1989) Journal of Dairy Research , vol.56 , pp. 61-68
    • Ono, T.1    Kohno, H.2    Odagiri, S.3    Takagi, T.4
  • 186
    • 0012120609 scopus 로고
    • A traveler's view of Outer Mongolia
    • Ørskov E.R. A traveler's view of Outer Mongolia. Outlook on Agriculture 1995, 24:127-129.
    • (1995) Outlook on Agriculture , vol.24 , pp. 127-129
    • Ørskov, E.R.1
  • 189
    • 66149152736 scopus 로고    scopus 로고
    • Mare milk
    • Blackwell Publishing, Oxford, UK, Y.W. Park, F.W. Haenlein (Eds.)
    • Park Y.W., Zhang H., Zhang B., Zhang L. Mare milk. Handbook of non-bovine mammals 2006, 275-296. Blackwell Publishing, Oxford, UK. Y.W. Park, F.W. Haenlein (Eds.).
    • (2006) Handbook of non-bovine mammals , pp. 275-296
    • Park, Y.W.1    Zhang, H.2    Zhang, B.3    Zhang, L.4
  • 190
    • 81255181034 scopus 로고    scopus 로고
    • Goat milk
    • Blackwell Publishing, Oxford, UK, Y.W. Park, F.W. Haenlein (Eds.)
    • Park Y.W., Zhang H., Zhang B., Zhang L. Goat milk. Handbook of non-bovine mammals 2006, 11-135. Blackwell Publishing, Oxford, UK. Y.W. Park, F.W. Haenlein (Eds.).
    • (2006) Handbook of non-bovine mammals , pp. 11-135
    • Park, Y.W.1    Zhang, H.2    Zhang, B.3    Zhang, L.4
  • 191
    • 0345436424 scopus 로고
    • Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry
    • Paulson M., Dejmek P. Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry. Journal of Dairy Science 1990, 73:590-600.
    • (1990) Journal of Dairy Science , vol.73 , pp. 590-600
    • Paulson, M.1    Dejmek, P.2
  • 192
    • 31144454094 scopus 로고    scopus 로고
    • Chemical-physical characteristics and fatty acid composition of mare's milk
    • Pelizzola V., Contarini G., Povolo M., Giangiacomo R. Chemical-physical characteristics and fatty acid composition of mare's milk. Milchwissenschaft 2006, 61:33-36.
    • (2006) Milchwissenschaft , vol.61 , pp. 33-36
    • Pelizzola, V.1    Contarini, G.2    Povolo, M.3    Giangiacomo, R.4
  • 193
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin
    • Pellegrini A., Dettling C., Thomas U., Hunziker P. Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochimica et Biophysica Acta 2001, 1526:131-140.
    • (2001) Biochimica et Biophysica Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 194
    • 0029302371 scopus 로고
    • Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review
    • Pérez M.D., Calvo M. Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. Journal of Dairy Science 1995, 78:978-988.
    • (1995) Journal of Dairy Science , vol.78 , pp. 978-988
    • Pérez, M.D.1    Calvo, M.2
  • 195
    • 0027549546 scopus 로고
    • Comparison of the ability to bind ligands of β-lactoglobulin and serum albumin from ruminant and non-ruminant species
    • Pérez M.D., Puyol P., Ena J.M., Calvo M. Comparison of the ability to bind ligands of β-lactoglobulin and serum albumin from ruminant and non-ruminant species. Journal of Dairy Research 1993, 60:55-63.
    • (1993) Journal of Dairy Research , vol.60 , pp. 55-63
    • Pérez, M.D.1    Puyol, P.2    Ena, J.M.3    Calvo, M.4
  • 197
    • 69349102184 scopus 로고    scopus 로고
    • Casein-derived bioactive peptides: biological effects, industrial uses, safety aspects and regulatory status
    • Phelan M., Aherne A., Fitzgerald R.J., O'Brien N.M. Casein-derived bioactive peptides: biological effects, industrial uses, safety aspects and regulatory status. International Dairy Journal 2009, 19:643-654.
    • (2009) International Dairy Journal , vol.19 , pp. 643-654
    • Phelan, M.1    Aherne, A.2    Fitzgerald, R.J.3    O'Brien, N.M.4
  • 199
  • 200
    • 77954834788 scopus 로고    scopus 로고
    • The influence of some factors on solids content in mare's milk
    • Pieszka M., Kulisa M. The influence of some factors on solids content in mare's milk. Roczniki Naukowe Zootechniki 2003, 17:513-516.
    • (2003) Roczniki Naukowe Zootechniki , vol.17 , pp. 513-516
    • Pieszka, M.1    Kulisa, M.2
  • 202
    • 0028557973 scopus 로고
    • Characterization of O-linked glycosylation motifs in the glycopeptide domain of bovine κ-casein
    • 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.
    • (1994) Glycobiology , vol.4 , pp. 837-844
    • Pisano, A.1    Packer, N.H.2    Redmond, J.W.3    Williams, K.L.4    Gooley, A.A.5
  • 203
    • 0033081678 scopus 로고    scopus 로고
    • Structural features of a peptide corresponding to human κ-casein residues 84-101 by H-nuclear magnetic resonance spectroscopy
    • Plowman J.E., Creamer L.K., Liddell M.J., Cross J.J. Structural features of a peptide corresponding to human κ-casein residues 84-101 by H-nuclear magnetic resonance spectroscopy. Journal of Dairy Research 1999, 66:53-63.
    • (1999) Journal of Dairy Research , vol.66 , pp. 53-63
    • Plowman, J.E.1    Creamer, L.K.2    Liddell, M.J.3    Cross, J.J.4
  • 204
    • 41849125311 scopus 로고    scopus 로고
    • Studies of casein micelle structure: the past and the present
    • Qi P.X. Studies of casein micelle structure: the past and the present. Lait 2007, 87:363-383.
    • (2007) Lait , vol.87 , pp. 363-383
    • Qi, P.X.1
  • 205
    • 0022649985 scopus 로고
    • Bacteriostatic activity of bovine milk lactoferrin against mastitic bacteria
    • Rainhard P. Bacteriostatic activity of bovine milk lactoferrin against mastitic bacteria. Veterinary Microbiology 1986, 11:387-392.
    • (1986) Veterinary Microbiology , vol.11 , pp. 387-392
    • Rainhard, P.1
  • 207
    • 0017892680 scopus 로고
    • Taurine and other free amino acids in milk of man and other mammals
    • Rassin D.K., Sturman J.A., Gaull G.E. Taurine and other free amino acids in milk of man and other mammals. Early Human Development 1978, 2(1):1-13.
    • (1978) Early Human Development , vol.2 , Issue.1 , pp. 1-13
    • Rassin, D.K.1    Sturman, J.A.2    Gaull, G.E.3
  • 212
    • 65949123742 scopus 로고    scopus 로고
    • Llama milk
    • Blackwell Publishing,, Oxford, UK, Y.W. Park, F.W. Haenlein (Eds.)
    • Rosenberg M. Llama milk. Handbook of non-bovine mammals 2006, 383-391. Blackwell Publishing,, Oxford, UK. Y.W. Park, F.W. Haenlein (Eds.).
    • (2006) Handbook of non-bovine mammals , pp. 383-391
    • Rosenberg, M.1
  • 213
    • 1542339542 scopus 로고    scopus 로고
    • Fermentation as a method of food processing: production of organic acids, pH-development and microbial growth in fermenting cereals
    • Sahlin, P. (1999). Fermentation as a method of food processing: production of organic acids, pH-development and microbial growth in fermenting cereals. (pp 9-19). Licentiate thesis. Division of Applied Nutrition and Food Chemistry, Lund University.
    • (1999) Licentiate thesis. Division of Applied Nutrition and Food Chemistry, Lund University , pp. 9-19
    • Sahlin, P.1
  • 214
    • 0026887671 scopus 로고
    • Variations and distributions of O-glycosidically linked sugar chains in bovine κ-casein
    • 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.
    • (1992) Journal of Dairy Science , vol.75 , pp. 1768-1774
    • Saito, T.1    Itoh, T.2
  • 216
    • 39049142993 scopus 로고    scopus 로고
    • A study of Lusitano mare lactation curve with Wood's model
    • Santos A.S., Silvestre A.M. A study of Lusitano mare lactation curve with Wood's model. Journal of Dairy Science 2008, 91:760-766.
    • (2008) Journal of Dairy Science , vol.91 , pp. 760-766
    • Santos, A.S.1    Silvestre, A.M.2
  • 220
    • 3142586885 scopus 로고    scopus 로고
    • β-Lactoglobulin
    • Kluwer Academic/Plenum Publishers, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • Sawyer L. β-Lactoglobulin. Proteins 2003, Vol. 1:319-386. Kluwer Academic/Plenum Publishers, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 319-386
    • Sawyer, L.1
  • 221
    • 0028829497 scopus 로고
    • Raising the pH of the pepsin-catalyzed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates
    • Schmidt D.G., Meijer R.J., Slangen C.J., van Beresteijn E.C. Raising the pH of the pepsin-catalyzed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates. Clinical and Experimental Allergy 1995, 25:1007-1017.
    • (1995) Clinical and Experimental Allergy , vol.25 , pp. 1007-1017
    • Schmidt, D.G.1    Meijer, R.J.2    Slangen, C.J.3    van Beresteijn, E.C.4
  • 224
    • 0034494479 scopus 로고    scopus 로고
    • Effects of milk-derived bioactives: an overview
    • Shah N.P. Effects of milk-derived bioactives: an overview. British Journal of Nutrition 2000, 84:S3-S10.
    • (2000) British Journal of Nutrition , vol.84
    • Shah, N.P.1
  • 229
    • 0028533570 scopus 로고
    • Comparative study of the iron-binding strengths of equine, bovine and human lactoferrins
    • Shimazaki K.I., Oota K., Nitta K., Ke Y. Comparative study of the iron-binding strengths of equine, bovine and human lactoferrins. Journal of Dairy Research 1994, 61:563-566.
    • (1994) Journal of Dairy Research , vol.61 , pp. 563-566
    • Shimazaki, K.I.1    Oota, K.2    Nitta, K.3    Ke, Y.4
  • 234
    • 0034543508 scopus 로고    scopus 로고
    • Association of the quadruply phosphorylated β-casein from human milk with the nonphosphorylated form
    • Sood S.M., Slattery C.W. Association of the quadruply phosphorylated β-casein from human milk with the nonphosphorylated form. Journal of Dairy Science 2000, 83:2766-2770.
    • (2000) Journal of Dairy Science , vol.83 , pp. 2766-2770
    • Sood, S.M.1    Slattery, C.W.2
  • 236
    • 0033152954 scopus 로고    scopus 로고
    • Expression, purification, and characterization of the recombinant calcium-binding equine lysozyme secreted by the filamentous fungus Aspergillus niger: comparisons with the production of hen and human lysozymes
    • Spencer A., Morozov-Roche L.A., Noppe W., McKenzie D.A., Jeenes D.J., Joniau M., et al. Expression, purification, and characterization of the recombinant calcium-binding equine lysozyme secreted by the filamentous fungus Aspergillus niger: comparisons with the production of hen and human lysozymes. Protein Expression and Purification 1999, 16:171-180.
    • (1999) Protein Expression and Purification , vol.16 , pp. 171-180
    • Spencer, A.1    Morozov-Roche, L.A.2    Noppe, W.3    McKenzie, D.A.4    Jeenes, D.J.5    Joniau, M.6
  • 237
    • 0033406832 scopus 로고    scopus 로고
    • Allergy to mammalian proteins: at the borderline between foreign and self?
    • Spitzauer S. Allergy to mammalian proteins: at the borderline between foreign and self?. International Archives of Allergy and Immunology 1999, 120:259-269.
    • (1999) International Archives of Allergy and Immunology , vol.120 , pp. 259-269
    • Spitzauer, S.1
  • 238
    • 0034466191 scopus 로고    scopus 로고
    • Cloning of a marsupial kappa-casein cDNA from the brushtail possum (Trichosurus vulpecula)
    • Stasiuk S.X., Summers E.L., Demmer J. Cloning of a marsupial kappa-casein cDNA from the brushtail possum (Trichosurus vulpecula). Reproduction, Fertility and Development 2000, 12:215-222.
    • (2000) Reproduction, Fertility and Development , vol.12 , pp. 215-222
    • Stasiuk, S.X.1    Summers, E.L.2    Demmer, J.3
  • 240
    • 0023973089 scopus 로고
    • Freeze-dried mares' milk and its potential use in infant and dietetic food products
    • Stoyanova L.G., Abramova L.A., Ladoto K.S. Freeze-dried mares' milk and its potential use in infant and dietetic food products. Voprosy Pitaniia 1988, 2:64-67.
    • (1988) Voprosy Pitaniia , vol.2 , pp. 64-67
    • Stoyanova, L.G.1    Abramova, L.A.2    Ladoto, K.S.3
  • 242
    • 33745808525 scopus 로고    scopus 로고
    • Fermented milks: types and standards of identity
    • Academic Press, London, UK, H. Roginski, J.A. Fuquay, P.F. Fox (Eds.)
    • Surono I.S., Hosono A. Fermented milks: types and standards of identity. Encyclopedia of dairy sciences 2003, 1018-1069. Academic Press, London, UK. H. Roginski, J.A. Fuquay, P.F. Fox (Eds.).
    • (2003) Encyclopedia of dairy sciences , pp. 1018-1069
    • Surono, I.S.1    Hosono, A.2
  • 243
    • 4143054391 scopus 로고    scopus 로고
    • Chemistry of caseins
    • Kluwer Academic/Plenum Publishers, New York, NY, USA, P.F. Fox, P.L.H. McSweeney (Eds.) Advanced dairy chemistry
    • Swaisgood H.F. Chemistry of caseins. Proteins 2003, Vol. 1:139-202. Kluwer Academic/Plenum Publishers, New York, NY, USA. 3rd ed. P.F. Fox, P.L.H. McSweeney (Eds.).
    • (2003) Proteins , vol.1 , pp. 139-202
    • Swaisgood, H.F.1
  • 244
    • 0037137186 scopus 로고    scopus 로고
    • Stabilization of protein by replacement of a fluctuating loop: structural analysis of a chimera of bovine α-lactalbumin and equine lysozyme
    • Tada M., Kobashiqawa Y., Mizuguchi M., Miura K., Kuono T., Kumaki Y., et al. Stabilization of protein by replacement of a fluctuating loop: structural analysis of a chimera of bovine α-lactalbumin and equine lysozyme. Biochemistry 2002, 41:13807-13813.
    • (2002) Biochemistry , vol.41 , pp. 13807-13813
    • Tada, M.1    Kobashiqawa, Y.2    Mizuguchi, M.3    Miura, K.4    Kuono, T.5    Kumaki, Y.6
  • 246
    • 0000519535 scopus 로고
    • Immunologic and allergic properties of cows' milk proteins in humans
    • Taylor S.L. Immunologic and allergic properties of cows' milk proteins in humans. Journal of Food Protection 1986, 49:239-250.
    • (1986) Journal of Food Protection , vol.49 , pp. 239-250
    • Taylor, S.L.1
  • 248
    • 41449095849 scopus 로고    scopus 로고
    • Changes in physical properties of bovine milk from the colostum period to early lactation
    • Tsioulpas A., Grandison A.S., Lewis M.J. Changes in physical properties of bovine milk from the colostum period to early lactation. Journal of Dairy Science 2007, 90:5012-5017.
    • (2007) Journal of Dairy Science , vol.90 , pp. 5012-5017
    • Tsioulpas, A.1    Grandison, A.S.2    Lewis, M.J.3
  • 249
    • 0026567045 scopus 로고
    • Crystallographic studies on a calcium-binding lysozyme from equine milk at 2.5 Å resolution
    • Tsuge H., Ago H., Noma M., Nitta K., Sugai S., Miyano M. Crystallographic studies on a calcium-binding lysozyme from equine milk at 2.5 Å resolution. Journal of Biochemistry 1992, 111:141-143.
    • (1992) Journal of Biochemistry , vol.111 , pp. 141-143
    • Tsuge, H.1    Ago, H.2    Noma, M.3    Nitta, K.4    Sugai, S.5    Miyano, M.6
  • 250
    • 54949134797 scopus 로고    scopus 로고
    • Diet composition and milk characteristics of Mediterranean water buffaloes reared in Southeastern Italy during spring season
    • Article #165. Retrieved 13.10.09, from
    • Tufarelli V., Dario M., Laudadio V. Diet composition and milk characteristics of Mediterranean water buffaloes reared in Southeastern Italy during spring season. Livestock Research for Rural Development 2008, 20. Article #165. Retrieved 13.10.09, from. http://www.lrrd.org/lrrd20/10/tufa20165.htm.
    • (2008) Livestock Research for Rural Development , vol.20
    • Tufarelli, V.1    Dario, M.2    Laudadio, V.3
  • 251
    • 84981868943 scopus 로고
    • Digestibility of milk as affected by various types of treatment
    • Turner A.W. Digestibility of milk as affected by various types of treatment. Food Research International 1945, 10:52-59.
    • (1945) Food Research International , vol.10 , pp. 52-59
    • Turner, A.W.1
  • 254
    • 0020119070 scopus 로고
    • Isolation and characterization of β- and γ-caseins in horse milk
    • Visser S., Jenness R., Mullin R.J. Isolation and characterization of β- and γ-caseins in horse milk. Biochemistry Journal 1982, 203:131-139.
    • (1982) Biochemistry Journal , vol.203 , pp. 131-139
    • Visser, S.1    Jenness, R.2    Mullin, R.J.3
  • 255
    • 0023050655 scopus 로고
    • 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
    • Vreeman H.J., Visser S., Slangen C.J., van Riel J.A.M. 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. Biochemistry Journal 1986, 240:87-97.
    • (1986) Biochemistry Journal , vol.240 , pp. 87-97
    • Vreeman, H.J.1    Visser, S.2    Slangen, C.J.3    van Riel, J.A.M.4
  • 258
    • 85025797643 scopus 로고
    • On the stability of casein micelles
    • Walstra P. On the stability of casein micelles. Journal of Dairy Science 1990, 73:1965-1979.
    • (1990) Journal of Dairy Science , vol.73 , pp. 1965-1979
    • Walstra, P.1
  • 261
    • 0009333710 scopus 로고
    • Further observations on lactose stimulation of the gastrointestinal absorption of calcium and strontium in the rat
    • Wasserman R.H., Langemann F.W. Further observations on lactose stimulation of the gastrointestinal absorption of calcium and strontium in the rat. Journal of Nutrition 1960, 70:377-384.
    • (1960) Journal of Nutrition , vol.70 , pp. 377-384
    • Wasserman, R.H.1    Langemann, F.W.2
  • 262
    • 0023838367 scopus 로고
    • Structural, histochemical and biochemical observations on horse milk-fat-globule membranes and casein micelles
    • Welsch U., Buchheim W., Schumacher U., Schinko I., Patton S. Structural, histochemical and biochemical observations on horse milk-fat-globule membranes and casein micelles. Histochemistry 1988, 88:357-365.
    • (1988) Histochemistry , vol.88 , pp. 357-365
    • Welsch, U.1    Buchheim, W.2    Schumacher, U.3    Schinko, I.4    Patton, S.5
  • 263
    • 0002282844 scopus 로고
    • Lactation and feeding patterns in different species
    • Bailliere Tindall Publishers, London, UK, D.L.M. Freed (Ed.)
    • Widdowson E.M. Lactation and feeding patterns in different species. Health hazards of milk 1984, 85-90. Bailliere Tindall Publishers, London, UK. D.L.M. Freed (Ed.).
    • (1984) Health hazards of milk , pp. 85-90
    • Widdowson, E.M.1
  • 264
    • 33750942819 scopus 로고    scopus 로고
    • Effect of β-lactotensin on acute stress and fear memory
    • Yamauchi R., Wada E., Yamada D., Yoshikawa M., Wada K. Effect of β-lactotensin on acute stress and fear memory. Peptides 2006, 27:3176-3182.
    • (2006) Peptides , vol.27 , pp. 3176-3182
    • Yamauchi, R.1    Wada, E.2    Yamada, D.3    Yoshikawa, M.4    Wada, K.5
  • 266
    • 0028310402 scopus 로고
    • Protein and nitrogen composition of equine (Equus caballus) milk during early lactation
    • A
    • Zicker S.C., Lönnerdal B. Protein and nitrogen composition of equine (Equus caballus) milk during early lactation. Comparative Biochemistry and Physiology 1994, 108A:411-421.
    • (1994) Comparative Biochemistry and Physiology , vol.108 , pp. 411-421
    • Zicker, S.C.1    Lönnerdal, B.2


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