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Volumn 93, Issue 2, 2010, Pages 437-455

Invited review: Physiological properties of bioactive peptides obtained from whey proteins

Author keywords

Bioactivity; Bovine; Peptide; Whey

Indexed keywords

MILK PROTEIN; PEPTIDE; WHEY PROTEIN;

EID: 77949290825     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2009-2566     Document Type: Review
Times cited : (281)

References (143)
  • 1
    • 0032240057 scopus 로고    scopus 로고
    • Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion
    • Abubakar A., Saito T., Kitazawa H., Kawai Y., Itoh T. Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion. J. Dairy Sci. 1998, 81:3131-3138.
    • (1998) J. Dairy Sci. , vol.81 , pp. 3131-3138
    • Abubakar, A.1    Saito, T.2    Kitazawa, H.3    Kawai, Y.4    Itoh, T.5
  • 2
    • 0037721339 scopus 로고    scopus 로고
    • Lactoferrin and lactoferricin inhibit Herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir
    • Andersen J.H., Jenssen H., Gutterberg T.J. Lactoferrin and lactoferricin inhibit Herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir. Antiviral Res. 2003, 58:209-215.
    • (2003) Antiviral Res. , vol.58 , pp. 209-215
    • Andersen, J.H.1    Jenssen, H.2    Gutterberg, T.J.3
  • 3
    • 0034960102 scopus 로고    scopus 로고
    • Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomelogavirus into human fibroblasts
    • Andersen J.H., Osbakk S.A., Vorland L.H., Travik T., Gutterberg T.J. Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomelogavirus into human fibroblasts. Antiviral Res. 2001, 51:141-149.
    • (2001) Antiviral Res. , vol.51 , pp. 141-149
    • Andersen, J.H.1    Osbakk, S.A.2    Vorland, L.H.3    Travik, T.4    Gutterberg, T.J.5
  • 5
    • 0000480144 scopus 로고    scopus 로고
    • Thermal stabilization of β-lactoblobulin by whey peptide factions
    • Barbeau J., Gauthier S.F., Pouliot Y. Thermal stabilization of β-lactoblobulin by whey peptide factions. J. Agric. Food Chem. 1996, 44:3939-3945.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 3939-3945
    • Barbeau, J.1    Gauthier, S.F.2    Pouliot, Y.3
  • 7
    • 0031127344 scopus 로고    scopus 로고
    • Isolation and biological properties of osteopontin from bovine milk
    • Bayless K.J., David G.E., Meininger G.A. Isolation and biological properties of osteopontin from bovine milk. Protein Expr. Purif. 1997, 9:309-314.
    • (1997) Protein Expr. Purif. , vol.9 , pp. 309-314
    • Bayless, K.J.1    David, G.E.2    Meininger, G.A.3
  • 8
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W., Takase M., Wakabayashi H., Kawase K., Tomita M. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 1992, 73:472-479.
    • (1992) J. Appl. Bacteriol. , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 11
    • 0028309575 scopus 로고
    • Antifungal properties of lactoferricin B, a peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W., Yamauchi K., Wakabayashi H., Takase M., Takakura N., Shimamura S. Antifungal properties of lactoferricin B, a peptide derived from the N-terminal region of bovine lactoferrin. Lett. Appl. Microbiol. 1994, 18:230-233.
    • (1994) Lett. Appl. Microbiol. , vol.18 , pp. 230-233
    • Bellamy, W.1    Yamauchi, K.2    Wakabayashi, H.3    Takase, M.4    Takakura, N.5    Shimamura, S.6
  • 12
    • 0023176333 scopus 로고
    • Immunostimulating properties and three-dimensional structure of two tripeptides from human and cow caseins
    • Berthou J., Migliore-Samour D., Lifchitz A., Delettre J., Floch F., Jolles P. Immunostimulating properties and three-dimensional structure of two tripeptides from human and cow caseins. FEBS Lett. 1987, 218:55-58.
    • (1987) FEBS Lett. , vol.218 , pp. 55-58
    • Berthou, J.1    Migliore-Samour, D.2    Lifchitz, A.3    Delettre, J.4    Floch, F.5    Jolles, P.6
  • 13
    • 0000304332 scopus 로고
    • Effect of caseinomacropeptide (CMP) of cholecystokinin (CCK) release in rats
    • Beucher M., Levenez F., Yvon Y., Corring T. Effect of caseinomacropeptide (CMP) of cholecystokinin (CCK) release in rats. Reprod. Nutr. Dev. 1994, 34:613-614.
    • (1994) Reprod. Nutr. Dev. , vol.34 , pp. 613-614
    • Beucher, M.1    Levenez, F.2    Yvon, Y.3    Corring, T.4
  • 14
    • 33645053239 scopus 로고    scopus 로고
    • Food-protein enzymatic hydrolysates possess both antimicrobial and immunostimulatory activities: A " cause and effect" theory of bifunctionality
    • Biziulevicius G.A., Kislukhina O.V., Kazlauskaite J., Zukaite V. Food-protein enzymatic hydrolysates possess both antimicrobial and immunostimulatory activities: A " cause and effect" theory of bifunctionality. FEMS Immunol. Med. Microbiol. 2006, 46:131-138.
    • (2006) FEMS Immunol. Med. Microbiol. , vol.46 , pp. 131-138
    • Biziulevicius, G.A.1    Kislukhina, O.V.2    Kazlauskaite, J.3    Zukaite, V.4
  • 15
    • 0033136017 scopus 로고    scopus 로고
    • Continuous hydrolysis of goat whey in an ultrafiltration reactor: Generation of alpha-lactorphin
    • Bordenave S., Sannier F., Ricart G., Piot J.M. Continuous hydrolysis of goat whey in an ultrafiltration reactor: Generation of alpha-lactorphin. Prep. Biochem. Biotechnol. 1999, 29:189-202.
    • (1999) Prep. Biochem. Biotechnol. , vol.29 , pp. 189-202
    • Bordenave, S.1    Sannier, F.2    Ricart, G.3    Piot, J.M.4
  • 16
    • 0000205599 scopus 로고
    • Nutritional and antigenic characterization of an enzymatic whey protein hydrolysate
    • Boza J.J., Martínez-Augustin O., Gil A. Nutritional and antigenic characterization of an enzymatic whey protein hydrolysate. J. Agric. Food Chem. 1995, 43:872-875.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 872-875
    • Boza, J.J.1    Martínez-Augustin, O.2    Gil, A.3
  • 17
    • 0034490342 scopus 로고    scopus 로고
    • Biological activities of bovine glycomacropeptide
    • Brody E.P. Biological activities of bovine glycomacropeptide. Br. J. Nutr. 2000, 84:39-46.
    • (2000) Br. J. Nutr. , vol.84 , pp. 39-46
    • Brody, E.P.1
  • 18
    • 3142527103 scopus 로고    scopus 로고
    • Antibacterial activity of lactophoricin, a synthetic 23-residue peptide derived from the sequence of bovine milk component-3 of proteose peptone
    • Campagna S., Mathot A.-G., Fleury Y., Girardet J.-M., Gaillard J.-L. Antibacterial activity of lactophoricin, a synthetic 23-residue peptide derived from the sequence of bovine milk component-3 of proteose peptone. J. Dairy Sci. 2004, 87:1621-1626.
    • (2004) J. Dairy Sci. , vol.87 , pp. 1621-1626
    • Campagna, S.1    Mathot, A.-G.2    Fleury, Y.3    Girardet, J.-M.4    Gaillard, J.-L.5
  • 19
    • 0032854339 scopus 로고    scopus 로고
    • β-Lactoglobulin hydrolysis. 1. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and Staphylococcus aureus V8 protease
    • Cassens P.W.J.R., Visser S., Gruppen H., Voragen A.G.J. β-Lactoglobulin hydrolysis. 1. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and Staphylococcus aureus V8 protease. J. Agric. Food Chem. 1999, 47:2973-2979.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2973-2979
    • Cassens, P.W.J.R.1    Visser, S.2    Gruppen, H.3    Voragen, A.G.J.4
  • 21
    • 0019332139 scopus 로고
    • Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence
    • Cheung H.S., Wang F.L., Ondetti M.A., Sabo E.F., Cushman D.W. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. J. Biol. Chem. 1980, 225:401-407.
    • (1980) J. Biol. Chem. , vol.225 , pp. 401-407
    • Cheung, H.S.1    Wang, F.L.2    Ondetti, M.A.3    Sabo, E.F.4    Cushman, D.W.5
  • 22
    • 0000022216 scopus 로고
    • Bioactive peptides derived from food proteins
    • Chiba H., Yoshikawa M. Bioactive peptides derived from food proteins. Kagaku To Seibutsu 1991, 29:454-458.
    • (1991) Kagaku To Seibutsu , vol.29 , pp. 454-458
    • Chiba, H.1    Yoshikawa, M.2
  • 23
    • 34648819856 scopus 로고    scopus 로고
    • Enzyme-induced aggregation and gelation of proteins
    • Creusot N., Gruppen H. Enzyme-induced aggregation and gelation of proteins. Biotechnol. Adv. 2006, 25:597-601.
    • (2006) Biotechnol. Adv. , vol.25 , pp. 597-601
    • Creusot, N.1    Gruppen, H.2
  • 24
    • 0032432558 scopus 로고    scopus 로고
    • Osteopontin expression and function: Role in bone remodelling
    • Denhardt D.T., Noda M. Osteopontin expression and function: Role in bone remodelling. J. Cell. Biochem. 1998, 30-31:92-102.
    • (1998) J. Cell. Biochem. , pp. 92-102
    • Denhardt, D.T.1    Noda, M.2
  • 25
    • 0037399626 scopus 로고    scopus 로고
    • Heparin-interacting sites of bovine lactoferrin are involved in anti-adenovirus activity
    • di Biase A.M., Pietrantoni A., Tinari A. Heparin-interacting sites of bovine lactoferrin are involved in anti-adenovirus activity. J. Med. Virol. 2003, 69:495-502.
    • (2003) J. Med. Virol. , vol.69 , pp. 495-502
    • di Biase, A.M.1    Pietrantoni, A.2    Tinari, A.3
  • 26
    • 33646452597 scopus 로고    scopus 로고
    • Peptides released from acid goat whey by a yeast-lactobacillus association isolated from cheese microflora
    • Didelot S., Bordenave-Juchereau S., Rosenfeld E., Piot J.-M., Sannier F. Peptides released from acid goat whey by a yeast-lactobacillus association isolated from cheese microflora. J. Dairy Res. 2006, 6:163-170.
    • (2006) J. Dairy Res. , vol.6 , pp. 163-170
    • Didelot, S.1    Bordenave-Juchereau, S.2    Rosenfeld, E.3    Piot, J.-M.4    Sannier, F.5
  • 27
    • 0031115106 scopus 로고    scopus 로고
    • Antibacterial peptides of bovine lactoferrin 494: Purification and characterization
    • Dionysius D.A., Milne J.M. Antibacterial peptides of bovine lactoferrin 494: Purification and characterization. J. Dairy Sci. 1997, 80:667-674.
    • (1997) J. Dairy Sci. , vol.80 , pp. 667-674
    • Dionysius, D.A.1    Milne, J.M.2
  • 28
    • 0030288545 scopus 로고    scopus 로고
    • Influence of glycosylation on content of both micelle-stabilizing ability and biological properties of the C-terminal fragments of cow's κ-casein
    • Dziuba J., Minkiewicz P. Influence of glycosylation on content of both micelle-stabilizing ability and biological properties of the C-terminal fragments of cow's κ-casein. Int. Dairy J. 1996, 6:1017-1044.
    • (1996) Int. Dairy J. , vol.6 , pp. 1017-1044
    • Dziuba, J.1    Minkiewicz, P.2
  • 29
    • 0030115568 scopus 로고    scopus 로고
    • Characteristics and potential uses of the casein macropeptide
    • el-Salam A.M.H., el-Shibiny S., Buchheim W. Characteristics and potential uses of the casein macropeptide. Int. Dairy J. 1996, 6:327-341.
    • (1996) Int. Dairy J. , vol.6 , pp. 327-341
    • el-Salam, A.M.H.1    el-Shibiny, S.2    Buchheim, W.3
  • 30
    • 0030094236 scopus 로고    scopus 로고
    • Antibacterial activity of lactoferricin, lysozyme and EDTA against Salmonella enteritidis
    • Facon M.J., Sakura B.J. Antibacterial activity of lactoferricin, lysozyme and EDTA against Salmonella enteritidis. Int. Dairy J. 1996, 6:303-313.
    • (1996) Int. Dairy J. , vol.6 , pp. 303-313
    • Facon, M.J.1    Sakura, B.J.2
  • 31
    • 0040937831 scopus 로고    scopus 로고
    • Lactokinins: Whey protein-derived ACE inhibitory peptides
    • FitzGerald R.J., Meisel H. Lactokinins: Whey protein-derived ACE inhibitory peptides. Nahrung/Food 1999, 43:165-167.
    • (1999) Nahrung/Food , vol.43 , pp. 165-167
    • FitzGerald, R.J.1    Meisel, H.2
  • 32
    • 0023929672 scopus 로고
    • Enhancement of phagocytic activity of human monocytic-macrophagic cells by immunostimulating peptides from human casein
    • Gattegno L., Migliore-Samour D., Saffar L., Jolles P. Enhancement of phagocytic activity of human monocytic-macrophagic cells by immunostimulating peptides from human casein. Immunol. Lett. 1988, 18:27-31.
    • (1988) Immunol. Lett. , vol.18 , pp. 27-31
    • Gattegno, L.1    Migliore-Samour, D.2    Saffar, L.3    Jolles, P.4
  • 33
    • 2342544490 scopus 로고    scopus 로고
    • Functional and biological properties of peptides obtained by enzymatic hydrolysis of whey proteins
    • Gauthier S.F., Pouliot Y. Functional and biological properties of peptides obtained by enzymatic hydrolysis of whey proteins. J. Dairy Sci. 2003, 86:78-87.
    • (2003) J. Dairy Sci. , vol.86 , pp. 78-87
    • Gauthier, S.F.1    Pouliot, Y.2
  • 34
    • 0000710259 scopus 로고
    • Enzymatic conditions of an in vitro method to study protein digestion
    • Gauthier S.F., Vachon C., Savoie L. Enzymatic conditions of an in vitro method to study protein digestion. J. Food Sci. 1986, 51:960-964.
    • (1986) J. Food Sci. , vol.51 , pp. 960-964
    • Gauthier, S.F.1    Vachon, C.2    Savoie, L.3
  • 36
    • 0027650986 scopus 로고
    • Study of a mechanism of lipolysis inhibition by bovine milk proteose peptone component-3
    • Girardet J.M., Linden G., Loye S., Courthaudon J.L., Lorient D. Study of a mechanism of lipolysis inhibition by bovine milk proteose peptone component-3. J. Dairy Sci. 1993, 76:2156-2163.
    • (1993) J. Dairy Sci. , vol.76 , pp. 2156-2163
    • Girardet, J.M.1    Linden, G.2    Loye, S.3    Courthaudon, J.L.4    Lorient, D.5
  • 38
    • 0032821714 scopus 로고    scopus 로고
    • Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens
    • Groenink J., Walgreen-Weterings E., van't Hof W., Veerman E.C., Amerongen A.V.N. Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens. FEMS Microbiol. Lett. 1999, 179:217-222.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 217-222
    • Groenink, J.1    Walgreen-Weterings, E.2    van't Hof, W.3    Veerman, E.C.4    Amerongen, A.V.N.5
  • 39
  • 40
    • 0035709562 scopus 로고    scopus 로고
    • Identification of peptide ligands generated by combinatorial chemistry that bind α-lactalbumin
    • Gurgel P.V., Carbonell R.G., Swaisgood H.E. Identification of peptide ligands generated by combinatorial chemistry that bind α-lactalbumin. Sep. Sci. Technol. 2001, 36:2411-2431.
    • (2001) Sep. Sci. Technol. , vol.36 , pp. 2411-2431
    • Gurgel, P.V.1    Carbonell, R.G.2    Swaisgood, H.E.3
  • 42
    • 0002360297 scopus 로고    scopus 로고
    • Bovine lactoferrin is more efficient than bovine lactoferricin in inhibiting HSV-I/II replication in vitro
    • Elsevier Science, Amsterdam, the Netherlands, K. Shimazaki (Ed.)
    • Hammer J., Haheim H., Gutterberg T.J. Bovine lactoferrin is more efficient than bovine lactoferricin in inhibiting HSV-I/II replication in vitro. Lactoferrin: Structure, Functions, and Applications 2000, 239-243. Elsevier Science, Amsterdam, the Netherlands. K. Shimazaki (Ed.).
    • (2000) Lactoferrin: Structure, Functions, and Applications , pp. 239-243
    • Hammer, J.1    Haheim, H.2    Gutterberg, T.J.3
  • 44
    • 0141610906 scopus 로고    scopus 로고
    • The influence of inadequate antimicrobial treatment of bloodstream infections on patient outcomes in the ICU setting
    • Ibrahim E.H., Sherman G., Ward S., Fraser V.J., Kollef M.H. The influence of inadequate antimicrobial treatment of bloodstream infections on patient outcomes in the ICU setting. Chest 2000, 118:146-155.
    • (2000) Chest , vol.118 , pp. 146-155
    • Ibrahim, E.H.1    Sherman, G.2    Ward, S.3    Fraser, V.J.4    Kollef, M.H.5
  • 49
    • 0027054727 scopus 로고
    • Specific binding sites on human phagocytic blood cells for Gly-Leu-Phe and Val-Glu-Pro-Ile-Pro-Tyr immunostimulating peptides from human milk proteins
    • Jaziri M., Migliore-Samour D., Casabianca-Pignède M.-R., Keddad K., Morgat J.-L., Jollès P. Specific binding sites on human phagocytic blood cells for Gly-Leu-Phe and Val-Glu-Pro-Ile-Pro-Tyr immunostimulating peptides from human milk proteins. Biochim. Biophys. Acta 1992, 1160:251-261.
    • (1992) Biochim. Biophys. Acta , vol.1160 , pp. 251-261
    • Jaziri, M.1    Migliore-Samour, D.2    Casabianca-Pignède, M.-R.3    Keddad, K.4    Morgat, J.-L.5    Jollès, P.6
  • 50
    • 0028868023 scopus 로고
    • Characterization of a bovine mammary gland PP3 cDNA reveals homology with mouse and rat adhesion molecule GlyCAM-1
    • Johnsen L.B., Sùrensen E.S., Petersen T.E., Berglund L. Characterization of a bovine mammary gland PP3 cDNA reveals homology with mouse and rat adhesion molecule GlyCAM-1. Biochim. Biophys. Acta 1995, 1260:116-118.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 116-118
    • Johnsen, L.B.1    Sùrensen, E.S.2    Petersen, T.E.3    Berglund, L.4
  • 51
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin
    • Kang J.H., Lee M.K., Kim K.L., Hahm K.-S. Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin. Int. J. Pept. Protein Res. 1996, 48:357-363.
    • (1996) Int. J. Pept. Protein Res. , vol.48 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.-S.4
  • 52
    • 0026815739 scopus 로고
    • Inhibition by lactoferrin and casein glycomacropeptide of binding of cholera toxin to its receptor
    • Kawasaki Y., Isoda H., Tanimoto M., Dosako S., Idota T., Ahiko K. Inhibition by lactoferrin and casein glycomacropeptide of binding of cholera toxin to its receptor. Biosci. Biotechnol. Biochem. 1992, 56:195-198.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 195-198
    • Kawasaki, Y.1    Isoda, H.2    Tanimoto, M.3    Dosako, S.4    Idota, T.5    Ahiko, K.6
  • 53
  • 54
    • 0029924099 scopus 로고    scopus 로고
    • Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins
    • Kayser H., Meisel H. Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Lett. 1996, 383:18-20.
    • (1996) FEBS Lett. , vol.383 , pp. 18-20
    • Kayser, H.1    Meisel, H.2
  • 55
    • 0011058457 scopus 로고
    • Indigenous milk enzymes
    • Applied Science Publishers, London, UK
    • Kitchen B.J. Indigenous milk enzymes. Developments in Dairy Chemistry 1985, 3:239. Applied Science Publishers, London, UK.
    • (1985) Developments in Dairy Chemistry , vol.3 , pp. 239
    • Kitchen, B.J.1
  • 56
    • 77949285454 scopus 로고    scopus 로고
    • Antibacterial and antiviral activities of whey proteins, the importance of whey and whey components in food and nutrition
    • Whey Conf., Munich, Germany
    • Korhonen H. Antibacterial and antiviral activities of whey proteins, the importance of whey and whey components in food and nutrition. Proc. 3rd Int 2001, 303-321. Whey Conf., Munich, Germany.
    • (2001) Proc. 3rd Int , pp. 303-321
    • Korhonen, H.1
  • 59
    • 57649200652 scopus 로고    scopus 로고
    • The influence of whey protein and glycomacropeptide on satiety in adult humans
    • Lam S.M., Moughan P.J., Awati A., Morton H.R. The influence of whey protein and glycomacropeptide on satiety in adult humans. Physiol. Behav. 2009, 96:162-168.
    • (2009) Physiol. Behav. , vol.96 , pp. 162-168
    • Lam, S.M.1    Moughan, P.J.2    Awati, A.3    Morton, H.R.4
  • 60
    • 30344483133 scopus 로고    scopus 로고
    • Des hydrolysats protéiques pour développer des aliments santé
    • Langley-Danysz P. Des hydrolysats protéiques pour développer des aliments santé. RIA Technol. Veille. 1998, 581:38-40.
    • (1998) RIA Technol. Veille. , vol.581 , pp. 38-40
    • Langley-Danysz, P.1
  • 61
    • 2342572985 scopus 로고    scopus 로고
    • Immunoenhancing effects of bovine glycomacropeptide and its derivatives on the proliferative response and phagocytic activities of human macrophage-like cells U937
    • Li E.W., Mine Y. Immunoenhancing effects of bovine glycomacropeptide and its derivatives on the proliferative response and phagocytic activities of human macrophage-like cells U937. J. Agric. Food Chem. 2004, 52:2704-2708.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 2704-2708
    • Li, E.W.1    Mine, Y.2
  • 64
    • 0030202780 scopus 로고    scopus 로고
    • Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790
    • Maeno M., Yamamoto N., Takano T. Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790. J. Dairy Sci. 1996, 79:1316-1321.
    • (1996) J. Dairy Sci. , vol.79 , pp. 1316-1321
    • Maeno, M.1    Yamamoto, N.2    Takano, T.3
  • 66
    • 0002608688 scopus 로고
    • Casein macropeptide from whey-A new product opportunity
    • Marshall S.C. Casein macropeptide from whey-A new product opportunity. Food Res. Quart. 1991, 51:86-89.
    • (1991) Food Res. Quart. , vol.51 , pp. 86-89
    • Marshall, S.C.1
  • 69
    • 0029888252 scopus 로고    scopus 로고
    • Lactoferrin or a fragment thereof inhibits the endotoxin-induced interleukin-6 response in human monocytic cells
    • Mattsby-Balzer I., Roseanu A., Motas C., Elverfors J., Engberg I., Hanson L.A. Lactoferrin or a fragment thereof inhibits the endotoxin-induced interleukin-6 response in human monocytic cells. Pediatr. Res. 1996, 40:257-262.
    • (1996) Pediatr. Res. , vol.40 , pp. 257-262
    • Mattsby-Balzer, I.1    Roseanu, A.2    Motas, C.3    Elverfors, J.4    Engberg, I.5    Hanson, L.A.6
  • 70
    • 0242383511 scopus 로고    scopus 로고
    • The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures
    • McCann K.B., Lee A., Wan J., Roginski H., Coventry M.J. The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures. J. Appl. Microbiol. 2003, 95:1026-1033.
    • (2003) J. Appl. Microbiol. , vol.95 , pp. 1026-1033
    • McCann, K.B.1    Lee, A.2    Wan, J.3    Roginski, H.4    Coventry, M.J.5
  • 71
    • 0032076817 scopus 로고    scopus 로고
    • Overview on milk protein-derived peptides
    • Meisel H. Overview on milk protein-derived peptides. Int. Dairy J. 1998, 8:363-373.
    • (1998) Int. Dairy J. , vol.8 , pp. 363-373
    • Meisel, H.1
  • 72
    • 0038397187 scopus 로고    scopus 로고
    • Biofunctional peptides from milk proteins, mineral binding and cytomodulatory effects
    • Meisel H., FitzGerald R.J. Biofunctional peptides from milk proteins, mineral binding and cytomodulatory effects. Curr. Pharm. Des. 2003, 9:1289-1295.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1289-1295
    • Meisel, H.1    FitzGerald, R.J.2
  • 73
    • 0030375693 scopus 로고    scopus 로고
    • Bioactive peptides derived from milk proteins: Ingredients for functional foods?
    • Meisel H., Schlimme E. Bioactive peptides derived from milk proteins: Ingredients for functional foods?. Kieler Milchwirts. Forsch. 1996, 48:343-357.
    • (1996) Kieler Milchwirts. Forsch. , vol.48 , pp. 343-357
    • Meisel, H.1    Schlimme, E.2
  • 74
    • 1142265857 scopus 로고    scopus 로고
    • Immunomodulating effects of whey proteins and their enzymatic digests
    • Mercier A., Gauthier S.F., Fliss I. Immunomodulating effects of whey proteins and their enzymatic digests. Int. Dairy J. 2004, 14:175-183.
    • (2004) Int. Dairy J. , vol.14 , pp. 175-183
    • Mercier, A.1    Gauthier, S.F.2    Fliss, I.3
  • 76
    • 0001151974 scopus 로고
    • A multi compartmental dynamic computer-controlled model simulating the stomach and small intestine
    • Minekus M., Marteau P., Havenaar R., Huis in't Veld J.H.J. A multi compartmental dynamic computer-controlled model simulating the stomach and small intestine. ATLA 1995, 23:197-209.
    • (1995) ATLA , vol.23 , pp. 197-209
    • Minekus, M.1    Marteau, P.2    Havenaar, R.3    Huis in't Veld, J.H.J.4
  • 77
    • 0027251567 scopus 로고
    • Development of a 5-step multi-chamber reactor as a simulation of the human intestinal microbial ecosystem
    • Molly K., van de Woestyne M., Verstraete W. Development of a 5-step multi-chamber reactor as a simulation of the human intestinal microbial ecosystem. Appl. Microbiol. Biotechnol. 1993, 39:254-258.
    • (1993) Appl. Microbiol. Biotechnol. , vol.39 , pp. 254-258
    • Molly, K.1    van de Woestyne, M.2    Verstraete, W.3
  • 78
    • 0029937138 scopus 로고    scopus 로고
    • Synthetic peptides corresponding to α-LA and β-LG sequences with angiotensin-I-converting enzyme inhibitory activity
    • Mullally M.M., Meisel H., FitzGerald R.J. Synthetic peptides corresponding to α-LA and β-LG sequences with angiotensin-I-converting enzyme inhibitory activity. Biol. Chem. Hoppe Seyler 1996, 377:259-260.
    • (1996) Biol. Chem. Hoppe Seyler , vol.377 , pp. 259-260
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 79
    • 0031464182 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins
    • Mullally M.M., Meisel H., FitzGerald R.J. Angiotensin-I-converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins. Int. Dairy J. 1997, 7:299-303.
    • (1997) Int. Dairy J. , vol.7 , pp. 299-303
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 80
    • 3242782703 scopus 로고    scopus 로고
    • Structural analysis of a new anti-hypertensive peptide (β-lactosin B) isolated from a commercial whey product
    • Murakami M., Tonouchi H., Takahashi R., Kitazawa H., Kawai Y., Negishi H., Saito T. Structural analysis of a new anti-hypertensive peptide (β-lactosin B) isolated from a commercial whey product. J. Dairy Sci. 2004, 87:1967-1974.
    • (2004) J. Dairy Sci. , vol.87 , pp. 1967-1974
    • Murakami, M.1    Tonouchi, H.2    Takahashi, R.3    Kitazawa, H.4    Kawai, Y.5    Negishi, H.6    Saito, T.7
  • 82
    • 0029319296 scopus 로고
    • Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme
    • Nakamura Y., Yamamoto N., Sakai K., Takano T. Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme. J. Dairy Sci. 1995, 78:1253-1257.
    • (1995) J. Dairy Sci. , vol.78 , pp. 1253-1257
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Takano, T.4
  • 83
    • 0023757139 scopus 로고
    • Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyrene by caseinoglycopeptide derivatives
    • Neeser J.-R., Chambaz A., del Vedovo S., Prigent M.-J., Guggenheim B. Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyrene by caseinoglycopeptide derivatives. Infect. Immun. 1988, 56:3201-3208.
    • (1988) Infect. Immun. , vol.56 , pp. 3201-3208
    • Neeser, J.-R.1    Chambaz, A.2    del Vedovo, S.3    Prigent, M.-J.4    Guggenheim, B.5
  • 86
    • 0020002135 scopus 로고
    • Enzymes of the renin-angiotensin system and their inhibitors
    • Ondetti M.A., Cushman D.W. Enzymes of the renin-angiotensin system and their inhibitors. Annu. Rev. Biochem. 1982, 51:283-308.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 283-308
    • Ondetti, M.A.1    Cushman, D.W.2
  • 89
    • 0034107036 scopus 로고    scopus 로고
    • Peptides obtained by tryptic hydrolysis of bovine β-lactoglobulin induce specific oral tolerance in mice
    • Pecquet S., Bovetto L., Maynard F., Fritsché R. Peptides obtained by tryptic hydrolysis of bovine β-lactoglobulin induce specific oral tolerance in mice. J. Allergy Clin. Immunol. 2000, 105:514-521.
    • (2000) J. Allergy Clin. Immunol. , vol.105 , pp. 514-521
    • Pecquet, S.1    Bovetto, L.2    Maynard, F.3    Fritsché, R.4
  • 90
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterisation of four bactericidal domains in the bovine α-lactoglobulin
    • Pellegrini A., Dettling C., Thomas U., Hunziker P. Isolation and characterisation of four bactericidal domains in the bovine α-lactoglobulin. Biochim. Biophys. Acta 2000, 1526:131-140.
    • (2000) Biochim. Biophys. Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 91
    • 0033022708 scopus 로고    scopus 로고
    • Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule
    • Pellegrini A., Thomas U., Bramaz N., Hunziker P., von Fellenberg R. Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule. Biochim. Biophys. Acta 1999, 1426:439-448.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 439-448
    • Pellegrini, A.1    Thomas, U.2    Bramaz, N.3    Hunziker, P.4    von Fellenberg, R.5
  • 92
    • 0030024410 scopus 로고    scopus 로고
    • Continuous hydrolysis of whey proteins in a membrane recycle reactor
    • Perea A., Ugalde U. Continuous hydrolysis of whey proteins in a membrane recycle reactor. Enzyme Microb. Technol. 1996, 18:29-34.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 29-34
    • Perea, A.1    Ugalde, U.2
  • 94
    • 0034141231 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory properties of whey protein digests: Concentration and characterization of active peptides
    • Pihlanto-Leppälä A., Koskinen P., Piilola K., Tupasela T., Korhonen H. Angiotensin I-converting enzyme inhibitory properties of whey protein digests: Concentration and characterization of active peptides. J. Dairy Res. 2000, 67:53-64.
    • (2000) J. Dairy Res. , vol.67 , pp. 53-64
    • Pihlanto-Leppälä, A.1    Koskinen, P.2    Piilola, K.3    Tupasela, T.4    Korhonen, H.5
  • 95
    • 0031062335 scopus 로고    scopus 로고
    • Bioactive peptide derived from in vitro proteolysis of bovine β-lactoglobulin and its effect on smooth muscle
    • Pihlanto-Leppälä A., Paakkari I., Rinta-Koski M., Antila P. Bioactive peptide derived from in vitro proteolysis of bovine β-lactoglobulin and its effect on smooth muscle. J. Dairy Res. 1997, 64:149-155.
    • (1997) J. Dairy Res. , vol.64 , pp. 149-155
    • Pihlanto-Leppälä, A.1    Paakkari, I.2    Rinta-Koski, M.3    Antila, P.4
  • 96
    • 0032047290 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides from bovine milk proteins
    • Pihlanto-Leppälä A., Rokka T., Korhonen H. Angiotensin I-converting enzyme inhibitory peptides from bovine milk proteins. Int. Dairy J. 1998, 8:325-331.
    • (1998) Int. Dairy J. , vol.8 , pp. 325-331
    • Pihlanto-Leppälä, A.1    Rokka, T.2    Korhonen, H.3
  • 97
    • 39049181769 scopus 로고    scopus 로고
    • Effects of whey peptides on cardiovascular disease risk factors
    • Pins J.J., Keenan J.M. Effects of whey peptides on cardiovascular disease risk factors. J. Clin. Hypertens. 2006, 8:775-782.
    • (2006) J. Clin. Hypertens. , vol.8 , pp. 775-782
    • Pins, J.J.1    Keenan, J.M.2
  • 98
    • 0028821534 scopus 로고
    • Overview of proposed mechanisms for the hypocholesterolemic effect of soy
    • Potter S. Overview of proposed mechanisms for the hypocholesterolemic effect of soy. J. Nutr. 1995, 125:606-611.
    • (1995) J. Nutr. , vol.125 , pp. 606-611
    • Potter, S.1
  • 99
    • 1642316967 scopus 로고    scopus 로고
    • Stimulation of interleukin-10 production by acidic beta-lactoglobulin-derived peptides hydrolyzed with Lactobacillus paracasei NCC2461 peptidases
    • Prioult G., Pecquet S., Fliss I. Stimulation of interleukin-10 production by acidic beta-lactoglobulin-derived peptides hydrolyzed with Lactobacillus paracasei NCC2461 peptidases. Clin. Diagn. Lab. Immunol. 2004, 11:266-271.
    • (2004) Clin. Diagn. Lab. Immunol. , vol.11 , pp. 266-271
    • Prioult, G.1    Pecquet, S.2    Fliss, I.3
  • 100
    • 0033009966 scopus 로고    scopus 로고
    • Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin: In situ enzymatic hydrolysis on an ion-exchange membrane
    • Recio I., Visser S. Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin: In situ enzymatic hydrolysis on an ion-exchange membrane. J Chromatogr. 1999, 831:191-201.
    • (1999) J Chromatogr. , vol.831 , pp. 191-201
    • Recio, I.1    Visser, S.2
  • 101
    • 77949280264 scopus 로고    scopus 로고
    • Bone health compositions derived from milk. US patent US2004052860. New Zealand Dairy Board, assignee.
    • Reid I. R., J. Cornish, N. W. Haggarty, and K. P. Palmano. 2004. Bone health compositions derived from milk. US patent US2004052860. New Zealand Dairy Board, assignee.
    • (2004)
    • Reid, I.R.1    Cornish, J.2    Haggarty, .N.W.3    Palmano, K.P.4
  • 102
    • 33845942566 scopus 로고    scopus 로고
    • Physicochemical characterization and in vitro digestibility of β-lactoglobulin/β-Lg f142-148 complexes
    • Roufik S., Gauthier S.F., Sylvie L.T. Physicochemical characterization and in vitro digestibility of β-lactoglobulin/β-Lg f142-148 complexes. Int. Dairy J. 2007, 7:471-480.
    • (2007) Int. Dairy J. , vol.7 , pp. 471-480
    • Roufik, S.1    Gauthier, S.F.2    Sylvie, L.T.3
  • 103
    • 30344441808 scopus 로고    scopus 로고
    • In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin
    • Roufik S., Gauthier S.F., Turgeon S.L. In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin. Int. Dairy J. 2006, 16:294-302.
    • (2006) Int. Dairy J. , vol.16 , pp. 294-302
    • Roufik, S.1    Gauthier, S.F.2    Turgeon, S.L.3
  • 104
    • 67349176658 scopus 로고    scopus 로고
    • Effect of feeding whey peptide fractions on the immune response in healthy and Escherichia coli infected mice
    • Saint-Sauveur D., Gauthier S.F., Boutin Y., Montoni A., Fliss I. Effect of feeding whey peptide fractions on the immune response in healthy and Escherichia coli infected mice. Int. Dairy J. 2009, 19:537-544.
    • (2009) Int. Dairy J. , vol.19 , pp. 537-544
    • Saint-Sauveur, D.1    Gauthier, S.F.2    Boutin, Y.3    Montoni, A.4    Fliss, I.5
  • 105
    • 0034221181 scopus 로고    scopus 로고
    • Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese
    • Saito T., Nakamura T., Kitazawa H., Kawai Y., Itoh T. Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese. J. Dairy Sci. 2000, 83:1434-1440.
    • (2000) J. Dairy Sci. , vol.83 , pp. 1434-1440
    • Saito, T.1    Nakamura, T.2    Kitazawa, H.3    Kawai, Y.4    Itoh, T.5
  • 107
    • 0000361334 scopus 로고
    • Effects of processing on whey protein functionality
    • Schmidt R.H., Packardm V.S., Morris H.A. Effects of processing on whey protein functionality. J. Dairy Sci. 1984, 67:2723-2733.
    • (1984) J. Dairy Sci. , vol.67 , pp. 2723-2733
    • Schmidt, R.H.1    Packardm, V.S.2    Morris, H.A.3
  • 108
    • 0030307198 scopus 로고    scopus 로고
    • Incorporation of caseinoglycomacropeptide and caseinophosphopeptide into the salivary pellicle inhibits adherence of mutant streptococci
    • Schupbach P., Neeser J.R., Golliard M., Rouvet M., Guggenheim B. Incorporation of caseinoglycomacropeptide and caseinophosphopeptide into the salivary pellicle inhibits adherence of mutant streptococci. J. Dent. Res. 1996, 75:1779-1788.
    • (1996) J. Dent. Res. , vol.75 , pp. 1779-1788
    • Schupbach, P.1    Neeser, J.R.2    Golliard, M.3    Rouvet, M.4    Guggenheim, B.5
  • 110
    • 0034494479 scopus 로고    scopus 로고
    • Effects of milk-derived bioactives: An overview
    • Shah N.P. Effects of milk-derived bioactives: An overview. Br. J. Nutr. 2000, 84(Suppl. 1):S3-S10.
    • (2000) Br. J. Nutr. , vol.84 , Issue.1 SUPPL
    • Shah, N.P.1
  • 112
    • 0031869799 scopus 로고    scopus 로고
    • Antibacterial activity of bovine lactoferrin and its peptides against enterohaemorrhagic Escherichia coli O157 7
    • Shin K., Yamauchi K., Teraguchi S., Hayasawa H., Tomita M., Otsuka Y., Yamazaki S. Antibacterial activity of bovine lactoferrin and its peptides against enterohaemorrhagic Escherichia coli O157 7. Lett. Appl. Microbiol. 1998, 26:407-411.
    • (1998) Lett. Appl. Microbiol. , vol.26 , pp. 407-411
    • Shin, K.1    Yamauchi, K.2    Teraguchi, S.3    Hayasawa, H.4    Tomita, M.5    Otsuka, Y.6    Yamazaki, S.7
  • 114
    • 8844258885 scopus 로고    scopus 로고
    • Caseins as source of bioactive peptides
    • Silva S.V., Malcata F.X. Caseins as source of bioactive peptides. Int. Dairy J. 2004, 15:1-15.
    • (2004) Int. Dairy J. , vol.15 , pp. 1-15
    • Silva, S.V.1    Malcata, F.X.2
  • 115
    • 0036099441 scopus 로고    scopus 로고
    • Effect of long-term intake of milk products on blood pressure in hypertensive rats
    • Sipola M., Finckenberg P., Korpela R., Vapaatalo H., Nurminen M.-L. Effect of long-term intake of milk products on blood pressure in hypertensive rats. J. Dairy Res. 2002, 69:103-111.
    • (2002) J. Dairy Res. , vol.69 , pp. 103-111
    • Sipola, M.1    Finckenberg, P.2    Korpela, R.3    Vapaatalo, H.4    Nurminen, M.-L.5
  • 116
    • 0033828099 scopus 로고    scopus 로고
    • Bioactive peptides in dairy products, synthesis and interaction with proteolytic enzymes
    • Smacchi E., Gobbetti M. Bioactive peptides in dairy products, synthesis and interaction with proteolytic enzymes. Food Microbiol. 2000, 17:129-141.
    • (2000) Food Microbiol. , vol.17 , pp. 129-141
    • Smacchi, E.1    Gobbetti, M.2
  • 118
    • 0011175654 scopus 로고
    • Purification and characterization of three proteins from the proteose peptone fraction of bovine milk
    • Sorensen E.S., Petersen T. Purification and characterization of three proteins from the proteose peptone fraction of bovine milk. J. Dairy Res. 1993, 60:189-197.
    • (1993) J. Dairy Res. , vol.60 , pp. 189-197
    • Sorensen, E.S.1    Petersen, T.2
  • 119
    • 0031308826 scopus 로고    scopus 로고
    • The localization and multimeric nature of component PP3 in bovine milk: Purification and characterization of PP3 from caprine and ovine milks
    • Sorensen E.S., Rasmussen L.K., Moller L., Petersen T.E. The localization and multimeric nature of component PP3 in bovine milk: Purification and characterization of PP3 from caprine and ovine milks. J. Dairy Sci. 1997, 80:3176-3181.
    • (1997) J. Dairy Sci. , vol.80 , pp. 3176-3181
    • Sorensen, E.S.1    Rasmussen, L.K.2    Moller, L.3    Petersen, T.E.4
  • 122
    • 0038521043 scopus 로고    scopus 로고
    • Nutritional and physiological role of milk protein components
    • International Dairy Federation, Brussels, Belgium, 11-16
    • Tomé D., Ledoux N. Nutritional and physiological role of milk protein components. Dairy Foods in Health Bulletin of the International Dairy Federation 1998, 336. International Dairy Federation, Brussels, Belgium, 11-16.
    • (1998) Dairy Foods in Health Bulletin of the International Dairy Federation , vol.336
    • Tomé, D.1    Ledoux, N.2
  • 126
    • 14944369298 scopus 로고    scopus 로고
    • Lactoferrampin an antimicrobial peptide of bovine lactoferrin exhibits its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix facilitating N-terminal part
    • van der Kraan M.I.A., Nazmi K., Teeken A., Groenink J., van't Hoff W., Veerman E.C.I. Lactoferrampin an antimicrobial peptide of bovine lactoferrin exhibits its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix facilitating N-terminal part. J. Biol. Chem. 2005, 386:137-142.
    • (2005) J. Biol. Chem. , vol.386 , pp. 137-142
    • van der Kraan, M.I.A.1    Nazmi, K.2    Teeken, A.3    Groenink, J.4    van't Hoff, W.5    Veerman, E.C.I.6
  • 128
    • 21444435350 scopus 로고    scopus 로고
    • Different anti-Candida activities of two lactoferrin-derived peptides Lfpep and kaliocin-1
    • Viejo-Díaz M., Andrés M.T., Fierro J.F. Different anti-Candida activities of two lactoferrin-derived peptides Lfpep and kaliocin-1. Antimicrob. Agents Chemother. 2005, 49:2583-2588.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2583-2588
    • Viejo-Díaz, M.1    Andrés, M.T.2    Fierro, J.F.3
  • 129
    • 0036185339 scopus 로고    scopus 로고
    • Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides
    • Vogel H.J., Shibli D.J., Jing W., Lohmeiher-Vogel E.M., Epand R.F., Epand R.M. Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides. Biochem. Cell Biol. 2002, 80:49-63.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 49-63
    • Vogel, H.J.1    Shibli, D.J.2    Jing, W.3    Lohmeiher-Vogel, E.M.4    Epand, R.F.5    Epand, R.M.6
  • 130
    • 0032701261 scopus 로고    scopus 로고
    • Initial binding sites of antimicrobial peptides in Staphylococcus aureus and Escherichia coli
    • Vorland L.H., Ulvatne H., Rekdal O., Svendsen J.S. Initial binding sites of antimicrobial peptides in Staphylococcus aureus and Escherichia coli. Scand. J. Infect. Dis. 1999, 31:467-473.
    • (1999) Scand. J. Infect. Dis. , vol.31 , pp. 467-473
    • Vorland, L.H.1    Ulvatne, H.2    Rekdal, O.3    Svendsen, J.S.4
  • 131
    • 0030457861 scopus 로고    scopus 로고
    • Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents
    • Wakabayashi H., Abe S., Okutomi T., Tansho S., Kawase K., Yamaguchi H. Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents. Microbiol. Immunol. 1996, 40:821-825.
    • (1996) Microbiol. Immunol. , vol.40 , pp. 821-825
    • Wakabayashi, H.1    Abe, S.2    Okutomi, T.3    Tansho, S.4    Kawase, K.5    Yamaguchi, H.6
  • 132
    • 0032930276 scopus 로고    scopus 로고
    • N-Acylated and d-enantiomer derivatives of a nonamer core peptide of lactoferricin B showing improved antimicrobial activity
    • Wakabayashi H., Matsumoto H., Hashimoto K., Teraguchi S., Takase M., Hayasawa H. N-Acylated and d-enantiomer derivatives of a nonamer core peptide of lactoferricin B showing improved antimicrobial activity. Antimicrob. Agents Chemother. 1999, 43:1267-1269.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1267-1269
    • Wakabayashi, H.1    Matsumoto, H.2    Hashimoto, K.3    Teraguchi, S.4    Takase, M.5    Hayasawa, H.6
  • 133
    • 0038397204 scopus 로고    scopus 로고
    • Lactoferricin derived from milk protein lactoferrin
    • Wakabayashi H., Takase M., Tomita M. Lactoferricin derived from milk protein lactoferrin. Curr. Pharm. Des. 2003, 9:1277-1287.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1277-1287
    • Wakabayashi, H.1    Takase, M.2    Tomita, M.3
  • 135
    • 0032114248 scopus 로고    scopus 로고
    • Immunostimulation of murine spleen cells by materials associated with bovine milk protein fractions
    • Wong K.F., Middleton N., Montgomery M., Dey M., Carr R.I. Immunostimulation of murine spleen cells by materials associated with bovine milk protein fractions. J. Dairy Sci. 1998, 81:1825-1832.
    • (1998) J. Dairy Sci. , vol.81 , pp. 1825-1832
    • Wong, K.F.1    Middleton, N.2    Montgomery, M.3    Dey, M.4    Carr, R.I.5
  • 136
    • 0033161658 scopus 로고    scopus 로고
    • Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by Lactobacillus helveticus CPN4
    • Yamamoto N., Maeno M., Takano T. Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by Lactobacillus helveticus CPN4. J. Dairy Sci. 1999, 82:1388-1393.
    • (1999) J. Dairy Sci. , vol.82 , pp. 1388-1393
    • Yamamoto, N.1    Maeno, M.2    Takano, T.3
  • 137
    • 0002220941 scopus 로고
    • Biologically functional proteins of milk and peptides derived from milk proteins
    • Yamauchi K. Biologically functional proteins of milk and peptides derived from milk proteins. Bull. Int. Dairy Fed. 1992, 272:51-58.
    • (1992) Bull. Int. Dairy Fed. , vol.272 , pp. 51-58
    • Yamauchi, K.1
  • 138
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi K., Tomita M., Giehl T.J., Ellison R.T. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 1993, 61:719-728.
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison, R.T.4
  • 139
    • 0842309109 scopus 로고    scopus 로고
    • β-Lactotensin and neurotensin rapidly reduce serum cholesterol via NT2 receptor
    • Yamauchi R., Ohinata K., Yoshikawa M. β-Lactotensin and neurotensin rapidly reduce serum cholesterol via NT2 receptor. Peptides 2003, 24:1955-1961.
    • (2003) Peptides , vol.24 , pp. 1955-1961
    • Yamauchi, R.1    Ohinata, K.2    Yoshikawa, M.3
  • 140
    • 0041317810 scopus 로고    scopus 로고
    • Characterization of β-lactotensin a bioactive peptide derived from bovine β-lactoglobulin as a neurotensin agonist
    • Yamauchi R., Usui H., Yunden J., Takenaka Y., Tani F., Yoshikawa M. Characterization of β-lactotensin a bioactive peptide derived from bovine β-lactoglobulin as a neurotensin agonist. Biosci. Biotechnol. Biochem. 2003, 67:940-943.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 940-943
    • Yamauchi, R.1    Usui, H.2    Yunden, J.3    Takenaka, Y.4    Tani, F.5    Yoshikawa, M.6
  • 142
    • 0000304902 scopus 로고
    • In vitro simulation of gastric digestion of milk proteins: Comparison between in vitro and in vivo data
    • Yvon M., Beucher S., Scanff P., Thirouin S., Pelissier J.P. In vitro simulation of gastric digestion of milk proteins: Comparison between in vitro and in vivo data. J. Agric. Food Chem. 1992, 40:239-244.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 239-244
    • Yvon, M.1    Beucher, S.2    Scanff, P.3    Thirouin, S.4    Pelissier, J.P.5
  • 143
    • 0027318991 scopus 로고
    • Influence of dietary fish proteins on plasma and liver cholesterol concentrations in rats
    • Zhang X., Beynen A.C. Influence of dietary fish proteins on plasma and liver cholesterol concentrations in rats. Br. J. Nutr. 1993, 69:767-777.
    • (1993) Br. J. Nutr. , vol.69 , pp. 767-777
    • Zhang, X.1    Beynen, A.C.2


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