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Volumn 62, Issue 1, 2006, Pages

New insights in biologically active proteins and peptides derived from hen egg

Author keywords

Bioactive peptides; Chronic disease; Egg proteins; Hen; Human health; Nutraceuticals

Indexed keywords

ANIMALIA;

EID: 33645501006     PISSN: 00439339     EISSN: None     Source Type: Journal    
DOI: 10.1079/WPS200586     Document Type: Review
Times cited : (85)

References (76)
  • 1
    • 0033178535 scopus 로고    scopus 로고
    • Transferrins, the mechanism of iron release by ovotransferrin
    • ABDALLAH, F.B. and CHAHINE, J.M. (1999) Transferrins, the mechanism of iron release by ovotransferrin. European Journal of Biochemistry 263: 912-920.
    • (1999) European Journal of Biochemistry , vol.263 , pp. 912-920
    • Abdallah, F.B.1    Chahine, J.M.2
  • 2
    • 0041736102 scopus 로고    scopus 로고
    • Transferrins selectively cause ion efflux through bacterial and artificial membranes
    • AGUILERA, O., QUIROS, L.M. and FIERRO, J.F. (2003) Transferrins selectively cause ion efflux through bacterial and artificial membranes. FEBS Letter 548: 5-10.
    • (2003) FEBS Letter , vol.548 , pp. 5-10
    • Aguilera, O.1    Quiros, L.M.2    Fierro, J.F.3
  • 3
    • 0025374696 scopus 로고
    • Evaluation of the effects of antigen specific immunotherapy on chronic sinusitis in children with allergy
    • ASAKURA, K., KOJIMA, T., SHIRASAKI, H. and KATAURA, A. (1990) Evaluation of the effects of antigen specific immunotherapy on chronic sinusitis in children with allergy. Auris Nasus Larynx 17: 33-38.
    • (1990) Auris Nasus Larynx , vol.17 , pp. 33-38
    • Asakura, K.1    Kojima, T.2    Shirasaki, H.3    Kataura, A.4
  • 4
    • 0022692831 scopus 로고
    • Natural antimicrobial systems and their potential in food preservation of the future
    • BANKS, J.G., BOARD, R.G. and SPARKS, N.H.C, (1986) Natural antimicrobial systems and their potential in food preservation of the future. Biotechnology and Applied Biochemistry 8: 103-147.
    • (1986) Biotechnology and Applied Biochemistry , vol.8 , pp. 103-147
    • Banks, J.G.1    Board, R.G.2    Sparks, N.H.C.3
  • 5
    • 27744458123 scopus 로고    scopus 로고
    • Behaviour of Salmonella enteritidis in industrial egg white: Egg naturally contains factors inhibitory to salmonella growth
    • Sim, J. S.; Nakai, N.; Guenter, W., Eds; CAB International: Oxon, UK
    • BARON, F., FAUVEL, S. and GAUTIER, M. (2000) Behaviour of Salmonella enteritidis in industrial egg white: egg naturally contains factors inhibitory to salmonella growth. In: Egg Nutrition and Biotechnology; Sim, J. S.; Nakai, N.; Guenter, W., Eds; CAB International: Oxon, UK, pp. 417-430.
    • (2000) Egg Nutrition and Biotechnology , pp. 417-430
    • Baron, F.1    Fauvel, S.2    Gautier, M.3
  • 6
    • 0036812851 scopus 로고    scopus 로고
    • A lipoprotein-derived antimicrobial factor from hen-egg yolk is active against Streptococcus species
    • BRADY, D., GAINES, S., FENELON, L., MCPARTLIN J. and O'FARRELLY, C.A. (2002) A lipoprotein-derived antimicrobial factor from hen-egg yolk is active against Streptococcus species. Journal of Food Science 67: 3096-3103.
    • (2002) Journal of Food Science , vol.67 , pp. 3096-3103
    • Brady, D.1    Gaines, S.2    Fenelon, L.3    Mcpartlin, J.4    O'Farrelly, C.A.5
  • 8
    • 0000154785 scopus 로고
    • Isolation and composition of avian egg yolk granules and their constituents α- and β-lipovitellines
    • BURLEY, R.W. and COOK, W.H. (1961) Isolation and composition of avian egg yolk granules and their constituents α- and β-lipovitellines. Canadian Journal of Biochemical Physiology 39: 1295-1307.
    • (1961) Canadian Journal of Biochemical Physiology , vol.39 , pp. 1295-1307
    • Burley, R.W.1    Cook, W.H.2
  • 9
    • 0036812851 scopus 로고    scopus 로고
    • A lipoprotein-derived antimicrobial factor from hen-egg yolk is active against Streptococcus species
    • BRADY, D., GAINES, S., FENELON, L., MCPARTLIN, J. and O'FARRELLY, C.A. (2002) A lipoprotein-derived antimicrobial factor from hen-egg yolk is active against Streptococcus species. Journal of Food Science 67: 3096-3103.
    • (2002) Journal of Food Science , vol.67 , pp. 3096-3103
    • Brady, D.1    Gaines, S.2    Fenelon, L.3    Mcpartlin, J.4    O'Farrelly, C.A.5
  • 10
    • 0034049475 scopus 로고    scopus 로고
    • Peroral immunotherapy with yolk antibodies for the prevention and treatment of enteric infections
    • CARLANDER, D., KOLLBERG, H., WEJAKER, P.E. and LARSSON, A. (2000) Peroral immunotherapy with yolk antibodies for the prevention and treatment of enteric infections. Immunology Research 21: 1-6.
    • (2000) Immunology Research , vol.21 , pp. 1-6
    • Carlander, D.1    Kollberg, H.2    Wejaker, P.E.3    Larsson, A.4
  • 11
    • 27744503766 scopus 로고    scopus 로고
    • Purification of phosvitin from egg yolk and determination of its physiochemical properties
    • CHOI, I., JUNG, C., SEOG, H. and CHOI, H. (2004) Purification of phosvitin from egg yolk and determination of its physiochemical properties. Food Science and Biotechnology 13: 434-437.
    • (2004) Food Science and Biotechnology , vol.13 , pp. 434-437
    • Choi, I.1    Jung, C.2    Seog, H.3    Choi, H.4
  • 12
    • 0004841111 scopus 로고
    • Egg product yield trends from shell eggs
    • COTTERDLL, O.J. and GEIGER, G.S. (1977) Egg product yield trends from shell eggs. Poultry Science 56: 1027-1031.
    • (1977) Poultry Science , vol.56 , pp. 1027-1031
    • Cotterdll, O.J.1    Geiger, G.S.2
  • 13
    • 0027008578 scopus 로고
    • Experimental evaluation of preventative and therapeutic potential of lysozyme
    • DAS, S., BANERJEE, S. and GUPTA, J.D. (1992) Experimental evaluation of preventative and therapeutic potential of lysozyme. Chemotherapy 38: 350-357.
    • (1992) Chemotherapy , vol.38 , pp. 350-357
    • Das, S.1    Banerjee, S.2    Gupta, J.D.3
  • 14
    • 4444238114 scopus 로고    scopus 로고
    • Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis
    • DAVALOS, A., MIGUEL, M., BARTOLOME, B. and LOPEZ-FINDINO, R. (2004) Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection 67: 1939-1944.
    • (2004) Journal of Food Protection , vol.67 , pp. 1939-1944
    • Davalos, A.1    Miguel, M.2    Bartolome, B.3    Lopez-Findino, R.4
  • 15
    • 0037440425 scopus 로고    scopus 로고
    • Methylglyoxal-bovine serum albumin stimulates tumor necrosis factor alpha secretion in RAW 264.7 cells through activation of mitogen-activating protein kinase, nuclear factor kappaB and intracellular reactive oxygen species formation
    • FAN, X., SUBRAMANIAM, R., WEISSM, M.F. and MONNIER, V.M. (2003) Methylglyoxal-bovine serum albumin stimulates tumor necrosis factor alpha secretion in RAW 264.7 cells through activation of mitogen-activating protein kinase, nuclear factor kappaB and intracellular reactive oxygen species formation. Archives of Biochemistry and Biophysics 409: 274-286.
    • (2003) Archives of Biochemistry and Biophysics , vol.409 , pp. 274-286
    • Fan, X.1    Subramaniam, R.2    Weissm, M.F.3    Monnier, V.M.4
  • 16
    • 0029442621 scopus 로고
    • Potentiation of the antihypertensive activity of orally administered ovokinin, a vasorelaxing peptide derived from ovalbumin, by emulsification in egg phosphatidylcholine
    • FUJITA, H., SASAKI, R. and YOSHIKAWA, M. (1995a) Potentiation of the antihypertensive activity of orally administered ovokinin, a vasorelaxing peptide derived from ovalbumin, by emulsification in egg phosphatidylcholine. Bioscience Biotechnology and Biochemistry 59: 2344-2345.
    • (1995) Bioscience Biotechnology and Biochemistry , vol.59 , pp. 2344-2345
    • Fujita, H.1    Sasaki, R.2    Yoshikawa, M.3
  • 17
    • 0029095148 scopus 로고
    • Isolation and characterization of ovokinin, a bradykinin B1 agonist peptide derived from ovalbumin
    • FUJITA, H., USUI, H., KURAHASHI, K. and YOSHIKAWA, M. (1995b) Isolation and characterization of ovokinin, a bradykinin B1 agonist peptide derived from ovalbumin. Peptides 16: 785-790.
    • (1995) Peptides , vol.16 , pp. 785-790
    • Fujita, H.1    Usui, H.2    Kurahashi, K.3    Yoshikawa, M.4
  • 19
    • 0037220792 scopus 로고    scopus 로고
    • In vivo augmentation of tumor-specific CTL responses by class I/peptide antigen complexes on microspheres (large multivalent immunogen)
    • GOLDBERG, J., SHRIKANT, P. and MESCHER, M.F. (2003) In vivo augmentation of tumor-specific CTL responses by class I/peptide antigen complexes on microspheres (large multivalent immunogen). Journal of Immunology 170: 228-235.
    • (2003) Journal of Immunology , vol.170 , pp. 228-235
    • Goldberg, J.1    Shrikant, P.2    Mescher, M.F.3
  • 20
    • 0030632555 scopus 로고    scopus 로고
    • Passive immunization against dental plaque formation in humans: Effect of a mouth rinse containing egg yolk antibodies (IgY) specific to Streptococcus mutans
    • HATTA, H., TSUDA, K., OZEKI, M., KIM, M., YAMAMOTO, T., OTAKE, S., HOROSAWA, M., KATZ, J., CHILDERS, N.K. and MICHALEK, S.M. (1997) Passive immunization against dental plaque formation in humans: Effect of a mouth rinse containing egg yolk antibodies (IgY) specific to Streptococcus mutans. Caries Research 31: 268-274.
    • (1997) Caries Research , vol.31 , pp. 268-274
    • Hatta, H.1    Tsuda, K.2    Ozeki, M.3    Kim, M.4    Yamamoto, T.5    Otake, S.6    Horosawa, M.7    Katz, J.8    Childers, N.K.9    Michalek, S.M.10
  • 21
    • 0141564867 scopus 로고    scopus 로고
    • Enhanced tumor immunogenicity through coupling cytokine expression with antigen presentation
    • HE, X., TSANG, T.C., LUO, P., ZHANG, T. and HARRIS, D.T. (2003) Enhanced tumor immunogenicity through coupling cytokine expression with antigen presentation. Cancer Gene Therapy 10: 669-677.
    • (2003) Cancer Gene Therapy , vol.10 , pp. 669-677
    • He, X.1    Tsang, T.C.2    Luo, P.3    Zhang, T.4    Harris, D.T.5
  • 23
    • 0035725623 scopus 로고    scopus 로고
    • Novel B and T cell epitopes of chicken ovomucoid (Gal d 1) induce T cell secretion of EL-6, IL-13, and IFN-gamma
    • HOLEN, E., BOLANN, B. and ELSAYED, S. (2001) Novel B and T cell epitopes of chicken ovomucoid (Gal d 1) induce T cell secretion of EL-6, IL-13, and IFN-gamma. Clinical Experimental Allergy 31: 952-964.
    • (2001) Clinical Experimental Allergy , vol.31 , pp. 952-964
    • Holen, E.1    Bolann, B.2    Elsayed, S.3
  • 24
    • 10044223088 scopus 로고    scopus 로고
    • Suppressive effect of functional drinking yogurt containing specific egg yolk immunoglobulin on Helicobacter pylori in humans
    • HORIE, K., HORIE, N., ABDOU, A.M., YANG, J-O, YUN, S.S., CHUN, C.K., KIM, M. and HATTA, H. (2004) Suppressive effect of functional drinking yogurt containing specific egg yolk immunoglobulin on Helicobacter pylori in humans. Journal of Dairy Science 87: 4703-4079.
    • (2004) Journal of Dairy Science , vol.87 , pp. 4703-4079
    • Horie, K.1    Horie, N.2    Abdou, A.M.3    Yang, J.-O.4    Yun, S.S.5    Chun, C.K.6    Kim, M.7    Hatta, H.8
  • 25
    • 0034684272 scopus 로고    scopus 로고
    • Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism
    • IBRAHIM, H.R., SUGIMOTO, Y. and AOKI, T. (2000) Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochimica et Biophysica Acta 1523: 196-205.
    • (2000) Biochimica et Biophysica Acta , vol.1523 , pp. 196-205
    • Ibrahim, H.R.1    Sugimoto, Y.2    Aoki, T.3
  • 26
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • IBRAHIM, H.R., THOMAS, U. and PELLEGRINI, A. (2001) A helix-loop peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. Journal of Biological Chemistry 276: 43767-43774.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 27
  • 28
    • 0034055342 scopus 로고    scopus 로고
    • Preparation of novel functional oligophosphopeptides from hen egg yolk phosvitin
    • JIANG, B. and MINE, Y. (2000) Preparation of novel functional oligophosphopeptides from hen egg yolk phosvitin. Journal of Agricultural Food Chemistry 48: 990-994.
    • (2000) Journal of Agricultural Food Chemistry , vol.48 , pp. 990-994
    • Jiang, B.1    Mine, Y.2
  • 29
    • 0035348366 scopus 로고    scopus 로고
    • Phosphopeptides derived from hen egg yolk phosvitin: Effect of molecular size on the calcium-binding properties
    • JIANG, B. and MINE, Y. (2001) Phosphopeptides derived from hen egg yolk phosvitin: effect of molecular size on the calcium-binding properties. Bioscience Biotechnology and Biochemistry 65: 1187-1190.
    • (2001) Bioscience Biotechnology and Biochemistry , vol.65 , pp. 1187-1190
    • Jiang, B.1    Mine, Y.2
  • 30
    • 4444253800 scopus 로고    scopus 로고
    • Non-immunized egg yolk powder can suppress the colonization of Salmonella typhimurium, E. coli 0157:H7 and Campylobacter jejuni in laying hens
    • KASSAIFY, Z.G. and MINE, Y. (2004a) Non-immunized egg yolk powder can suppress the colonization of Salmonella typhimurium, E. coli 0157:H7 and Campylobacter jejuni in laying hens. Poultry Science 83: 1497-1506.
    • (2004) Poultry Science , vol.83 , pp. 1497-1506
    • Kassaify, Z.G.1    Mine, Y.2
  • 31
    • 20744459014 scopus 로고    scopus 로고
    • Identification of antiadhesive fractions in nonimmunized egg yolk powder: In vitro study
    • KASSAIFY, Z.G., Li, E.W.Y. and MINE, Y. (2005) Identification of antiadhesive fractions in nonimmunized egg yolk powder: In vitro study. Journal of Agricultural Food Chemistry 53: 4607-4614.
    • (2005) Journal of Agricultural Food Chemistry , vol.53 , pp. 4607-4614
    • Kassaify, Z.G.1    Li, E.W.Y.2    Mine, Y.3
  • 32
    • 3042697268 scopus 로고    scopus 로고
    • Effect of food protein supplements on Salmonella enteritidis infection and prevention in laying hens
    • KASSAIFY, Z.G. and MINE, Y. (2004b) Effect of food protein supplements on Salmonella enteritidis infection and prevention in laying hens. Poultry Science 83: 753-760.
    • (2004) Poultry Science , vol.83 , pp. 753-760
    • Kassaify, Z.G.1    Mine, Y.2
  • 35
    • 0038350759 scopus 로고    scopus 로고
    • Oral administration of specific yolk antibodies (IgY) may prevent Pseudomonas aeruginosa infections in patients with cystic fibrosis: A phase I feasibility study
    • KOLLBERG, H., CARLANDER, D., OLESEN, H., WEJAKER, P.E., JOHANNESSON, M. and LARSSON, A. (2003) Oral administration of specific yolk antibodies (IgY) may prevent Pseudomonas aeruginosa infections in patients with cystic fibrosis: A phase I feasibility study. Pediatric pulmonology 35: 433-440.
    • (2003) Pediatric Pulmonology , vol.35 , pp. 433-440
    • Kollberg, H.1    Carlander, D.2    Olesen, H.3    Wejaker, P.E.4    Johannesson, M.5    Larsson, A.6
  • 37
    • 12944330150 scopus 로고    scopus 로고
    • Avian egg antibodies: Basic and potential applications
    • KOVACS-NOLAN, J. and MINE, Y. (2004) Avian egg antibodies: Basic and potential applications. Avian Poultry Biology Review 15: 25-46.
    • (2004) Avian Poultry Biology Review , vol.15 , pp. 25-46
    • Kovacs-Nolan, J.1    Mine, Y.2
  • 40
  • 41
    • 85128156270 scopus 로고
    • The Chemistry of eggs and egg products
    • Stadelman, W. J.; Cotterill, O. J., Eds.; The Haworth Press, Inc.: New York, New York
    • LI-CHAN, E., POWRIE, W.D. and NAKAI, S. (1995) The Chemistry of eggs and egg products. In: Egg Science and Technology, 4th Edition; Stadelman, W. J.; Cotterill, O. J., Eds.; The Haworth Press, Inc.: New York, New York, pp. 105-175.
    • (1995) Egg Science and Technology, 4th Edition , pp. 105-175
    • Li-Chan, E.1    Powrie, W.D.2    Nakai, S.3
  • 43
    • 0022818205 scopus 로고
    • Characteristics of egg yolk phosvitin as an antioxidant for inhibiting metal-catalyzed phospholipid oxidations
    • LU, C.L. and BAKER, R. (1986) Characteristics of egg yolk phosvitin as an antioxidant for inhibiting metal-catalyzed phospholipid oxidations. Poultry Science 65: 2065-2070.
    • (1986) Poultry Science , vol.65 , pp. 2065-2070
    • Lu, C.L.1    Baker, R.2
  • 44
    • 0033042906 scopus 로고    scopus 로고
    • A novel anti-hypertensive peptide derived from ovalbumin induces nitric oxide-mediated vasorelaxation in an isolated SHR mesenteric artery
    • MATOBA, N., USUI, H., FUJITA, H. and YOSHIKAWA, M. (1999) A novel anti-hypertensive peptide derived from ovalbumin induces nitric oxide-mediated vasorelaxation in an isolated SHR mesenteric artery. FEBS Letter 452: 181-184.
    • (1999) FEBS Letter , vol.452 , pp. 181-184
    • Matoba, N.1    Usui, H.2    Fujita, H.3    Yoshikawa, M.4
  • 46
    • 4444253706 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory activity of peptides derived from egg white proteins by enzymatic hydrolysis
    • MIGUEL, M., RECIO, I., GOMEZ-RUIZ, J.A., RAMOS, M. and LOPEZ-FANDINO, R. (2004) Angiotensin I-converting enzyme inhibitory activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection 67: 1914-1920.
    • (2004) Journal of Food Protection , vol.67 , pp. 1914-1920
    • Miguel, M.1    Recio, I.2    Gomez-Ruiz, J.A.3    Ramos, M.4    Lopez-Fandino, R.5
  • 47
    • 1542347593 scopus 로고    scopus 로고
    • Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme
    • MINE, Y., MA, F. and LAURIAU, S. (2004) Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme. Journal of Agriculture and Food Chemistry 52: 1088-1094.
    • (2004) Journal of Agriculture and Food Chemistry , vol.52 , pp. 1088-1094
    • Mine, Y.1    Ma, F.2    Lauriau, S.3
  • 48
    • 0036203677 scopus 로고    scopus 로고
    • Egg ovomucin attenuates hypercholesterolemia in rats and inhibits cholesterol absorption in Caco-2 cells
    • NAGAOKA, S., MASAOKA, M., ZHANG, Q., HASEGAWA, M. and WATANABE, K. (2002) Egg ovomucin attenuates hypercholesterolemia in rats and inhibits cholesterol absorption in Caco-2 cells. Lipids 37: 267-272.
    • (2002) Lipids , vol.37 , pp. 267-272
    • Nagaoka, S.1    Masaoka, M.2    Zhang, Q.3    Hasegawa, M.4    Watanabe, K.5
  • 49
  • 50
    • 0030729849 scopus 로고    scopus 로고
    • Inhibition of proliferative responses of mouse spleen lymphocytes by lacto- and ovotransferrins
    • OTANI, H. and ODASHIMA, M. (1997) Inhibition of proliferative responses of mouse spleen lymphocytes by lacto- and ovotransferrins. Food Agriculture and Immunology 9: 193-202.
    • (1997) Food Agriculture and Immunology , vol.9 , pp. 193-202
    • Otani, H.1    Odashima, M.2
  • 51
    • 0033210821 scopus 로고    scopus 로고
    • In vitro down regulation of ICAM-1 and E-cadherin and in vitro reduction of lung metastases of TS/A adenocarcinoma by a lysozyme derivative
    • PACOR, S., GAGLIARD, R., DI DANIEL, E., VADORI, M. and SAVA, G. (1999) In vitro down regulation of ICAM-1 and E-cadherin and in vitro reduction of lung metastases of TS/A adenocarcinoma by a lysozyme derivative. International of Journal Molecular Medecine 4: 369-375.
    • (1999) International of Journal Molecular Medecine , vol.4 , pp. 369-375
    • Pacor, S.1    Gagliard, R.2    Di Daniel, E.3    Vadori, M.4    Sava, G.5
  • 53
    • 0033903248 scopus 로고    scopus 로고
    • Effect of lysozyme or modified lysozyme fragments on DNA and RNA synthesis and membrane permeability of Escherichia coli
    • PELLERGRINI, A., THOMAS, U., WILD, P., SCHRANER, E. and VON FELLENBERG, R. (2000) Effect of lysozyme or modified lysozyme fragments on DNA and RNA synthesis and membrane permeability of Escherichia coli. Microbiology Research 155: 69-77.
    • (2000) Microbiology Research , vol.155 , pp. 69-77
    • Pellergrini, A.1    Thomas, U.2    Wild, P.3    Schraner, E.4    Von Fellenberg, R.5
  • 55
    • 0025851402 scopus 로고
    • Observations on the antimetastatic action of lysozyme in mice bearing Lewis lung carcinoma
    • SAVA, G., CESCHIA, V., PACOR, S. and ZABUCCHI, G. (1991) Observations on the antimetastatic action of lysozyme in mice bearing Lewis lung carcinoma. Anticancer Research 11: 1109-1113.
    • (1991) Anticancer Research , vol.11 , pp. 1109-1113
    • Sava, G.1    Ceschia, V.2    Pacor, S.3    Zabucchi, G.4
  • 56
    • 0029622438 scopus 로고
    • Lysozyme stimulates lymphocyte response to ConA and IL-2 and potentiates 5-fluorouracil action on advanced carcinomas
    • SAVA, G., PACOR, S., DASIC, G. and BERGAMO, A. (1995) Lysozyme stimulates lymphocyte response to ConA and IL-2 and potentiates 5-fluorouracil action on advanced carcinomas. Anticancer Research 15: 1883-1888.
    • (1995) Anticancer Research , vol.15 , pp. 1883-1888
    • Sava, G.1    Pacor, S.2    Dasic, G.3    Bergamo, A.4
  • 57
    • 0029687177 scopus 로고    scopus 로고
    • Pharmacological aspects and therapeutic applications of lysozymes
    • SAVA, G. (1996) Pharmacological aspects and therapeutic applications of lysozymes. Experimental Science 75: 433-449.
    • (1996) Experimental Science , vol.75 , pp. 433-449
    • Sava, G.1
  • 58
    • 0036052918 scopus 로고    scopus 로고
    • Fighting infectious diseases with inhibitors of microbial adhesion to host tissues
    • SHARON, N. and OFEK, I. (2002) Fighting infectious diseases with inhibitors of microbial adhesion to host tissues. Critical Review of Food Science and Nutrition 42: 267-272.
    • (2002) Critical Review of Food Science and Nutrition , vol.42 , pp. 267-272
    • Sharon, N.1    Ofek, I.2
  • 59
    • 0035064161 scopus 로고    scopus 로고
    • Passive transfer of immunoglobulin Y to Streptococcus mutans glucan binding protein B can confer protection against experimental dental caries
    • SMITH, D.J., KING, W.F. and GODISKA, R. (2001) Passive transfer of immunoglobulin Y to Streptococcus mutans glucan binding protein B can confer protection against experimental dental caries. Infection and Immunity 69: 3135-3142.
    • (2001) Infection and Immunity , vol.69 , pp. 3135-3142
    • Smith, D.J.1    King, W.F.2    Godiska, R.3
  • 60
    • 0034213796 scopus 로고    scopus 로고
    • The mode of actions of lysozyme as an immunoglobulin production stimulating factor
    • SUGAHARA, T., MURAKAMI, F., YAMADA, Y. and SASAKI, T. (2000) The mode of actions of lysozyme as an immunoglobulin production stimulating factor. Biochimica et Biophysica Acta 1475: 27-34.
    • (2000) Biochimica et Biophysica Acta , vol.1475 , pp. 27-34
    • Sugahara, T.1    Murakami, F.2    Yamada, Y.3    Sasaki, T.4
  • 61
    • 0012398736 scopus 로고    scopus 로고
    • General chemical composition of hen eggs
    • Yamamoto, T.; Juneja, L. R.; Hatta, H.; Kim, M., Eds.; CRC Press, Inc.: New York, New York
    • SUGINO, H., NITODA, T. and JUNEJA, L.R. (1997) General chemical composition of hen eggs. In: Hen Eggs, Their Basic and Applied Science; Yamamoto, T.; Juneja, L. R.; Hatta, H.; Kim, M., Eds.; CRC Press, Inc.: New York, New York, pp. 13-24.
    • (1997) Hen Eggs, Their Basic and Applied Science , pp. 13-24
    • Sugino, H.1    Nitoda, T.2    Juneja, L.R.3
  • 62
    • 0031262210 scopus 로고    scopus 로고
    • Activation of macrophages by sulfated glycopeptides in ovomucin, yolk membrane, and chalazae in chicken eggs
    • TANIZAKI, H., TANAKA, H., IWATA, H. and KATO, A. (1997) Activation of macrophages by sulfated glycopeptides in ovomucin, yolk membrane, and chalazae in chicken eggs. Bioscience, Biotechnology and Biochemistry 61: 1883-1889.
    • (1997) Bioscience, Biotechnology and Biochemistry , vol.61 , pp. 1883-1889
    • Tanizaki, H.1    Tanaka, H.2    Iwata, H.3    Kato, A.4
  • 65
    • 0030246673 scopus 로고    scopus 로고
    • Differences in hemagglutination inhibition activity against bovine rotavirus and hen newcastle disease virus based on the subunits in hen egg white ovomucin
    • TSUGE, Y., SHIMOYAMADA, M. and WATANABE, K. (1996b) Differences in hemagglutination inhibition activity against bovine rotavirus and hen newcastle disease virus based on the subunits in hen egg white ovomucin. Bioscience, Biotechnology and Biochemistry 60: 1505-1506.
    • (1996) Bioscience, Biotechnology and Biochemistry , vol.60 , pp. 1505-1506
    • Tsuge, Y.1    Shimoyamada, M.2    Watanabe, K.3
  • 66
    • 0001046338 scopus 로고    scopus 로고
    • Structural features of newcastle disease virus- and anti-ovomucin antibody-binding glycopeptides from pronase-treated ovomucin
    • TSUGE, Y., SHIMOYAMADA, M. and WATANABE, K. (1997a) Structural features of newcastle disease virus- and anti-ovomucin antibody-binding glycopeptides from pronase-treated ovomucin. Journal of Agriculture and Food Chemistry 45: 2393-2398.
    • (1997) Journal of Agriculture and Food Chemistry , vol.45 , pp. 2393-2398
    • Tsuge, Y.1    Shimoyamada, M.2    Watanabe, K.3
  • 67
    • 0000350506 scopus 로고    scopus 로고
    • Bindings of ovomucin to newcastle disease virus and anti-ovomucin antibodies and its heat stability based on binding abilities
    • TSUGE, Y., SHIMOYAMADA, M. and WATANABE, K. (1997b) Bindings of ovomucin to newcastle disease virus and anti-ovomucin antibodies and its heat stability based on binding abilities. Journal of Agriculture and Food Chemistry 45: 4629-4634.
    • (1997) Journal of Agriculture and Food Chemistry , vol.45 , pp. 4629-4634
    • Tsuge, Y.1    Shimoyamada, M.2    Watanabe, K.3
  • 70
    • 0033572915 scopus 로고    scopus 로고
    • Chicken cystatin stimulates nitric oxide release from interferon-gamma-activated mouse peritoneal macrophages via cytokine synthesis
    • VERDOT, L., LALMANACH, G., VERCRUYSSE, V., HOEBEKE, J., GAUTHIER, F. and VRAY, B. (1999) Chicken cystatin stimulates nitric oxide release from interferon-gamma-activated mouse peritoneal macrophages via cytokine synthesis. European Journal of Biochemistry 266: 1111-1117.
    • (1999) European Journal of Biochemistry , vol.266 , pp. 1111-1117
    • Verdot, L.1    Lalmanach, G.2    Vercruysse, V.3    Hoebeke, J.4    Gauthier, F.5    Vray, B.6
  • 72
    • 0038010756 scopus 로고    scopus 로고
    • Primary immunodeficiencies caused by defects of cytokines and cytokine receptors
    • Korholz, D.; Kiess, W., Eds.; Humana Press Inc.: Totowa, New Jersey
    • WAHN, V. (2003) Primary immunodeficiencies caused by defects of cytokines and cytokine receptors. In: Methods in Molecular Biology: Cytokines and Colony Stimulating Factors: Methods and Protocols; Korholz, D.; Kiess, W., Eds.; Humana Press Inc.: Totowa, New Jersey, Vol. 215, pp. 3-12.
    • (2003) Methods in Molecular Biology: Cytokines and Colony Stimulating Factors: Methods and Protocols , vol.215 , pp. 3-12
    • Wahn, V.1
  • 73
    • 0001255351 scopus 로고    scopus 로고
    • Antitumor effects of pronase-treated fragments, glycopeptides, from ovomucin in hen egg white in a double grafted tumor system
    • WATANABE, K., YSUGE, Y., SHIMOYAMADA, M., OGAMA, N. and EBINA, T. (1998) Antitumor effects of pronase-treated fragments, glycopeptides, from ovomucin in hen egg white in a double grafted tumor system. Journal of Agriculture and Food Chemistry 46: 3033-3038.
    • (1998) Journal of Agriculture and Food Chemistry , vol.46 , pp. 3033-3038
    • Watanabe, K.1    Ysuge, Y.2    Shimoyamada, M.3    Ogama, N.4    Ebina, T.5
  • 76
    • 9844257355 scopus 로고
    • Studies on the optimum conditions to utilize biologically active peptides derived from food proteins
    • Yano, T; Matsuno, R.; Nakamura, K., Eds.; Blackie Academic and Professional: New York, New York
    • YOSHIKAWA, M. and FUJITA, H. (1994) Studies on the optimum conditions to utilize biologically active peptides derived from food proteins. In: Developments in Food Engineering; Yano, T; Matsuno, R.; Nakamura, K., Eds.; Blackie Academic and Professional: New York, New York, pp. 1053-1055.
    • (1994) Developments in Food Engineering , pp. 1053-1055
    • Yoshikawa, M.1    Fujita, H.2


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