메뉴 건너뛰기




Volumn 46, Issue 2, 2012, Pages 480-487

Ovotransferrin: Structure, bioactivities, and preparation

Author keywords

Antimicrobial activity; Bioactive peptides; Bioactivity; Functional food; Nutraceutical; Ovotransferrin; Preparation; Structure

Indexed keywords

ANTI-MICROBIAL ACTIVITY; BIOACTIVE PEPTIDES; FUNCTIONAL FOODS; NUTRACEUTICALS; OVOTRANSFERRIN; PREPARATION;

EID: 84858004731     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2011.07.012     Document Type: Article
Times cited : (131)

References (96)
  • 1
    • 0033178535 scopus 로고    scopus 로고
    • Transferrins, the mechanism of iron release by ovotransferrin
    • Abdallah F.B., Chahine J.M. Transferrins, the mechanism of iron release by ovotransferrin. European Journal of Biochemistry 1999, 263:912-920.
    • (1999) European Journal of Biochemistry , vol.263 , pp. 912-920
    • Abdallah, F.B.1    Chahine, J.M.2
  • 3
    • 85010170786 scopus 로고
    • Separation of ovotransferrin from egg white by immobilized metal affinity chromatography
    • Al-Mashikhi S.A., Nakai N. Separation of ovotransferrin from egg white by immobilized metal affinity chromatography. Agricultural and Biological Chemistry 1987, 51:2881-2887.
    • (1987) Agricultural and Biological Chemistry , vol.51 , pp. 2881-2887
    • Al-Mashikhi, S.A.1    Nakai, N.2
  • 4
    • 0028023255 scopus 로고
    • Two-step chromatographic procedure for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins
    • Awadé A.C., Moreau S., Mollé D., Brulé G., Maubois J.L. Two-step chromatographic procedure for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins. Journal of Chromatography. A 1994, 677:279-288.
    • (1994) Journal of Chromatography. A , vol.677 , pp. 279-288
    • Awadé, A.C.1    Moreau, S.2    Mollé, D.3    Brulé, G.4    Maubois, J.L.5
  • 5
    • 49949134880 scopus 로고
    • A simple and rapid procedure for preparation of large quantities of pure ovotransferrin
    • Azari P., Baugh R. A simple and rapid procedure for preparation of large quantities of pure ovotransferrin. Archives of Biochemistry 1967, 118:138-144.
    • (1967) Archives of Biochemistry , vol.118 , pp. 138-144
    • Azari, P.1    Baugh, R.2
  • 6
    • 3342963515 scopus 로고    scopus 로고
    • Lactoferrin and iron: Structural and dynamic aspects of binding and release
    • Baker H.M., Baker E.N. Lactoferrin and iron: Structural and dynamic aspects of binding and release. BioMetals 2004, 17:209-216.
    • (2004) BioMetals , vol.17 , pp. 209-216
    • Baker, H.M.1    Baker, E.N.2
  • 7
    • 0000154631 scopus 로고
    • Structure and reactivity of transferrins
    • Academic Press
    • Baker E.N., Sykes A.G. Structure and reactivity of transferrins. Advances in inorganic chemistry 1994, Vol. 41:389-463. Academic Press.
    • (1994) Advances in inorganic chemistry , vol.41 , pp. 389-463
    • Baker, E.N.1    Sykes, A.G.2
  • 8
    • 27744458123 scopus 로고    scopus 로고
    • Behaviour of Sallmonella enteritidis in industrial egg white: Egg naturally contains factors inhibitory to salmonella growth
    • CAB International, Oxon, J. Sim, N. Nakai, W. Guenter (Eds.)
    • Baron F., Fauvel S., Gautier M. Behaviour of Sallmonella enteritidis in industrial egg white: Egg naturally contains factors inhibitory to salmonella growth. Egg nutrition and biotechnology 2000, 417-430. CAB International, Oxon. J. Sim, N. Nakai, W. Guenter (Eds.).
    • (2000) Egg nutrition and biotechnology , pp. 417-430
    • Baron, F.1    Fauvel, S.2    Gautier, M.3
  • 9
    • 35748981775 scopus 로고    scopus 로고
    • Effect of ovotransferrin and lactoferrins on Chlamydophila psittaci adhesion and invasion in HD11 chicken macrophages
    • Beekman S.A., VanDroogenbroeck M.A.D., DeCock J.A. Effect of ovotransferrin and lactoferrins on Chlamydophila psittaci adhesion and invasion in HD11 chicken macrophages. Veterinary Research 2007, 38:729-739.
    • (2007) Veterinary Research , vol.38 , pp. 729-739
    • Beekman, S.A.1    VanDroogenbroeck, M.A.D.2    DeCock, J.A.3
  • 11
    • 0347988225 scopus 로고    scopus 로고
    • Natural antimicrobial systems/lysozyme and other proteins in eggs
    • San Diego: Academic Press Elsevier, R. Robinson (Ed.)
    • Charter E., Lagarde G. Natural antimicrobial systems/lysozyme and other proteins in eggs. Encyclopedia of food microbiology 2004, Vol. 1-3:1582-1587. San Diego: Academic Press Elsevier. R. Robinson (Ed.).
    • (2004) Encyclopedia of food microbiology , vol.1-3 , pp. 1582-1587
    • Charter, E.1    Lagarde, G.2
  • 13
    • 0018721460 scopus 로고
    • Organisation and sequence studies of the 17-piece chicken conalbumin gene
    • Cochet M., Gannon F., Hen R., Maroteaux L., Perrin F., Chambon P. Organisation and sequence studies of the 17-piece chicken conalbumin gene. Nature 1979, 282:567-574.
    • (1979) Nature , vol.282 , pp. 567-574
    • Cochet, M.1    Gannon, F.2    Hen, R.3    Maroteaux, L.4    Perrin, F.5    Chambon, P.6
  • 18
    • 0018792525 scopus 로고
    • Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin
    • Dorland L., Haverkamp J., Vliegenthart J.F.G., Spik G., Fournet B., Montreuil J. Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin. European Journal of Biochemistry 1979, 100:569-574.
    • (1979) European Journal of Biochemistry , vol.100 , pp. 569-574
    • Dorland, L.1    Haverkamp, J.2    Vliegenthart, J.F.G.3    Spik, G.4    Fournet, B.5    Montreuil, J.6
  • 20
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K., Cheung B.W.Y., Schröder H. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. Journal of Nutritional Biochemistry 2008, 19:643-654.
    • (2008) Journal of Nutritional Biochemistry , vol.19 , pp. 643-654
    • Erdmann, K.1    Cheung, B.W.Y.2    Schröder, H.3
  • 23
    • 0032760778 scopus 로고    scopus 로고
    • LKPNM: a prodrug-type ACE inhibitory peptide derived from fish protein
    • Fujita H., Yoshikawa M. LKPNM: a prodrug-type ACE inhibitory peptide derived from fish protein. Immunopharmacology 1999, 44:123-127.
    • (1999) Immunopharmacology , vol.44 , pp. 123-127
    • Fujita, H.1    Yoshikawa, M.2
  • 25
    • 34249946590 scopus 로고    scopus 로고
    • Ovotransferrin expression and release by chicken cell lines infected with Marek's disease virus
    • Giansanti F., Giardi M.F., Massucci M.T., Botti D., Antonini G. Ovotransferrin expression and release by chicken cell lines infected with Marek's disease virus. Biochemical Cell Biology 2007, 85:150-155.
    • (2007) Biochemical Cell Biology , vol.85 , pp. 150-155
    • Giansanti, F.1    Giardi, M.F.2    Massucci, M.T.3    Botti, D.4    Antonini, G.5
  • 27
    • 0036188350 scopus 로고    scopus 로고
    • Antiviral activity of ovotransferrin discloses an evolutionary strategy for the defensive activities of lactoferrin
    • Giansanti F., Rossi P., Massucci M.T., Botti D., Antonini G., Valenti P., et al. Antiviral activity of ovotransferrin discloses an evolutionary strategy for the defensive activities of lactoferrin. Biochemical Cell Biology 2002, 80:125-130.
    • (2002) Biochemical Cell Biology , vol.80 , pp. 125-130
    • Giansanti, F.1    Rossi, P.2    Massucci, M.T.3    Botti, D.4    Antonini, G.5    Valenti, P.6
  • 28
    • 0000317007 scopus 로고
    • Separation of three proteins from egg white
    • Guerin C., Brule G. Separation of three proteins from egg white. Sciences des Aliments 1992, 12:705-720.
    • (1992) Sciences des Aliments , vol.12 , pp. 705-720
    • Guerin, C.1    Brule, G.2
  • 31
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: From research to food applications
    • Hartmann R., Meisel H. Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology 2007, 18:163-169.
    • (2007) Current Opinion in Biotechnology , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 33
    • 0031550284 scopus 로고    scopus 로고
    • Development of a high-performance capillary isoelectric focusing technique with application to studies of microheterogeneity in chicken conalbumin
    • Huang T.L., Richards M. Development of a high-performance capillary isoelectric focusing technique with application to studies of microheterogeneity in chicken conalbumin. Journal of Chromatography. A 1997, 757:247-253.
    • (1997) Journal of Chromatography. A , vol.757 , pp. 247-253
    • Huang, T.L.1    Richards, M.2
  • 35
    • 0009004334 scopus 로고    scopus 로고
    • Insights into the structure-function relationships of ovalbumin, ovotransferrin, and lysozyme
    • CRC Press, Boca Raton, FL, T. Yamamoto, L.R. Juneja, H. Hatta, M. Kim (Eds.)
    • Ibrahim H.R. Insights into the structure-function relationships of ovalbumin, ovotransferrin, and lysozyme. Hen eggs their basic and applied science 1997, CRC Press, Boca Raton, FL. T. Yamamoto, L.R. Juneja, H. Hatta, M. Kim (Eds.).
    • (1997) Hen eggs their basic and applied science
    • Ibrahim, H.R.1
  • 36
  • 37
    • 33644881919 scopus 로고    scopus 로고
    • Ovotransferrin is a redox-dependent autoprocessing protein incorporation four consensus self-cleaving motifs flanking the two kringles
    • Ibrahim H.R., Haraguchi T., Aoki T. Ovotransferrin is a redox-dependent autoprocessing protein incorporation four consensus self-cleaving motifs flanking the two kringles. Biochimica et Biophysica Acta (BBA) - General subjects 2006, 1760:347-355.
    • (2006) Biochimica et Biophysica Acta (BBA) - General subjects , vol.1760 , pp. 347-355
    • Ibrahim, H.R.1    Haraguchi, T.2    Aoki, T.3
  • 38
    • 35348822093 scopus 로고    scopus 로고
    • Ovotransferrin possesses SOD-like superoxide anion scavenging activity that is promoted by copper and manganese binding
    • Ibrahim H.R., Hoq M.I., Aoki T. Ovotransferrin possesses SOD-like superoxide anion scavenging activity that is promoted by copper and manganese binding. International Journal of Biological Macromolecules 2007, 41:631-640.
    • (2007) International Journal of Biological Macromolecules , vol.41 , pp. 631-640
    • Ibrahim, H.R.1    Hoq, M.I.2    Aoki, T.3
  • 40
    • 72449167457 scopus 로고    scopus 로고
    • Novel anticancer activity of the autocleaved ovotransferrin against human colon and breast cancer cells
    • Ibrahim H.R., Kiyono T. Novel anticancer activity of the autocleaved ovotransferrin against human colon and breast cancer cells. Journal of Agricultural and Food Chemistry 2009, 57:11383-11390.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 11383-11390
    • Ibrahim, H.R.1    Kiyono, T.2
  • 41
    • 0020092046 scopus 로고
    • The complete nucleotide sequence of the chicken ovotransferrin mRNA
    • Jeltsch J.-M., Chambon P. The complete nucleotide sequence of the chicken ovotransferrin mRNA. European Journal of Biochemistry 1982, 122:291-295.
    • (1982) European Journal of Biochemistry , vol.122 , pp. 291-295
    • Jeltsch, J.-M.1    Chambon, P.2
  • 43
    • 46249098031 scopus 로고    scopus 로고
    • An economic and simple purification procedure for the large-scale production of ovotransferrin from egg white
    • Ko K.Y., Ahn D.U. An economic and simple purification procedure for the large-scale production of ovotransferrin from egg white. Poultry Science 2008, 87:1441-1450.
    • (2008) Poultry Science , vol.87 , pp. 1441-1450
    • Ko, K.Y.1    Ahn, D.U.2
  • 44
    • 49449104466 scopus 로고    scopus 로고
    • Effect of ethylenediaminetetraacetate and lysozyme on the antimicrobial activity of ovotransferrin against Listeria monocytogenes
    • Ko K.Y., Mendonca A.F., Ahn D.U. Effect of ethylenediaminetetraacetate and lysozyme on the antimicrobial activity of ovotransferrin against Listeria monocytogenes. Poultry Science 2008, 87:1649-1658.
    • (2008) Poultry Science , vol.87 , pp. 1649-1658
    • Ko, K.Y.1    Mendonca, A.F.2    Ahn, D.U.3
  • 45
    • 57049118092 scopus 로고    scopus 로고
    • Influence of zinc, sodium bicarbonate, and citric acid on the antibacterial activity of ovotransferrin against Escherichia coli O157:H7 and Listeria monocytogenes in model systems and ham
    • Ko K.Y., Mendonca A.F., Ahn D.U. Influence of zinc, sodium bicarbonate, and citric acid on the antibacterial activity of ovotransferrin against Escherichia coli O157:H7 and Listeria monocytogenes in model systems and ham. Poultry Science 2008, 87:2660-2670.
    • (2008) Poultry Science , vol.87 , pp. 2660-2670
    • Ko, K.Y.1    Mendonca, A.F.2    Ahn, D.U.3
  • 46
    • 63249135315 scopus 로고    scopus 로고
    • Ethylenediaminetetraacetate and lysozyme improves antimicrobial activities of ovotransferrin against Escherichia coli O157:H7
    • Ko K.Y., Mendonca A.F., Ismail H., Ahn D.U. Ethylenediaminetetraacetate and lysozyme improves antimicrobial activities of ovotransferrin against Escherichia coli O157:H7. Poultry Science 2009, 88:406-414.
    • (2009) Poultry Science , vol.88 , pp. 406-414
    • Ko, K.Y.1    Mendonca, A.F.2    Ismail, H.3    Ahn, D.U.4
  • 48
    • 0028835226 scopus 로고
    • Crystal structure of diferric hen ovotransferrin at 2.4Å resolution
    • Kurokawa H., Mikami B., Hirose M. Crystal structure of diferric hen ovotransferrin at 2.4Å resolution. Journal of Molecular Biology 1995, 254:196-207.
    • (1995) Journal of Molecular Biology , vol.254 , pp. 196-207
    • Kurokawa, H.1    Mikami, B.2    Hirose, M.3
  • 49
    • 0026735744 scopus 로고
    • The iron uptake mechanisms of enteropathogenic Escherichia coli: The use of haem and haemoglobin during growth in an iron-limited environment
    • Law D., Wilkie K.M., Freeman R., Gould F.K. The iron uptake mechanisms of enteropathogenic Escherichia coli: The use of haem and haemoglobin during growth in an iron-limited environment. Journal of Medical Microbiology 1992, 37:15-21.
    • (1992) Journal of Medical Microbiology , vol.37 , pp. 15-21
    • Law, D.1    Wilkie, K.M.2    Freeman, R.3    Gould, F.K.4
  • 50
    • 33646734243 scopus 로고    scopus 로고
    • One peptide derived from hen ovotransferrin as pro-drug to inhibit angiotensin converting enzyme
    • Lee N.-Y., Cheng J.-T., Enomoto T., Nakano Y. One peptide derived from hen ovotransferrin as pro-drug to inhibit angiotensin converting enzyme. Journal of Food and Drug Analysis 2006, 14:31-35.
    • (2006) Journal of Food and Drug Analysis , vol.14 , pp. 31-35
    • Lee, N.-Y.1    Cheng, J.-T.2    Enomoto, T.3    Nakano, Y.4
  • 53
    • 0028348559 scopus 로고
    • Calorimetric studies of serum transferrin and ovotransferrin. Estimates of domain interactions, and study of the kinetic complexities of ferric ion binding
    • Lin L.N., Mason A.B., Woodworth R.C., Brandts J.F. Calorimetric studies of serum transferrin and ovotransferrin. Estimates of domain interactions, and study of the kinetic complexities of ferric ion binding. Biochemistry 1994, 33:1881-1888.
    • (1994) Biochemistry , vol.33 , pp. 1881-1888
    • Lin, L.N.1    Mason, A.B.2    Woodworth, R.C.3    Brandts, J.F.4
  • 54
    • 0026696961 scopus 로고
    • Persistence of contamination of hen's egg albumen in vitro with Salmonella serotypes
    • Lock J.L., Board R.G. Persistence of contamination of hen's egg albumen in vitro with Salmonella serotypes. Epidemiology and Infection 1992, 108:389-396.
    • (1992) Epidemiology and Infection , vol.108 , pp. 389-396
    • Lock, J.L.1    Board, R.G.2
  • 55
    • 77953912348 scopus 로고    scopus 로고
    • A new approach for identification of novel antihypertensive peptides from egg proteins by QSAR and bioinformatics
    • Majumder K., Wu J. A new approach for identification of novel antihypertensive peptides from egg proteins by QSAR and bioinformatics. Food Research International 2010, 43:1371-1378.
    • (2010) Food Research International , vol.43 , pp. 1371-1378
    • Majumder, K.1    Wu, J.2
  • 58
    • 0018691450 scopus 로고
    • Transcriptional regulation of the ovalbumin and conalbumin genes by steroid hormones in chick oviduct
    • McKnight G.S., Palmiter R.D. Transcriptional regulation of the ovalbumin and conalbumin genes by steroid hormones in chick oviduct. The Journal of Biological Chemistry 1979, 254:9050-9058.
    • (1979) The Journal of Biological Chemistry , vol.254 , pp. 9050-9058
    • McKnight, G.S.1    Palmiter, R.D.2
  • 59
    • 0035876277 scopus 로고    scopus 로고
    • Domain closure mechanism in transferrins: new viewpoints about the hinge structure and motion as deduced from high resolution crystal structures of ovotransferrin N-lobe
    • Mizutani K., Mikami B., Hirose M. Domain closure mechanism in transferrins: new viewpoints about the hinge structure and motion as deduced from high resolution crystal structures of ovotransferrin N-lobe. Journal of Molecular Biology 2001, 309:937-947.
    • (2001) Journal of Molecular Biology , vol.309 , pp. 937-947
    • Mizutani, K.1    Mikami, B.2    Hirose, M.3
  • 62
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production
    • Murray B.A., FitzGerald R.J. Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production. Current Pharmaceutical Design 2007, 13:773-791.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 773-791
    • Murray, B.A.1    FitzGerald, R.J.2
  • 63
    • 0023916722 scopus 로고
    • Amino-terminal and carboxyl-terminal half-molecules of ovotransferrin: preparation by a novel procedure and their interactions
    • Oe H., Doi E., Hirose M. Amino-terminal and carboxyl-terminal half-molecules of ovotransferrin: preparation by a novel procedure and their interactions. Journal of Biochemistry 1988, 103:1066-1072.
    • (1988) Journal of Biochemistry , vol.103 , pp. 1066-1072
    • Oe, H.1    Doi, E.2    Hirose, M.3
  • 64
    • 77953479720 scopus 로고    scopus 로고
    • Co-extraction of egg white proteins using ion-exchange chromatography from ovomucin-removed egg whites
    • Omana D.A., Wang J., Wu J. Co-extraction of egg white proteins using ion-exchange chromatography from ovomucin-removed egg whites. Journal of Chromatography B 2010, 878:1771-1776.
    • (2010) Journal of Chromatography B , vol.878 , pp. 1771-1776
    • Omana, D.A.1    Wang, J.2    Wu, J.3
  • 65
    • 0030729849 scopus 로고    scopus 로고
    • Inhibition of proliferative responses of mouse spleen lymphocytes by lacto- and ovotransferrins
    • Otani H., Odashima M. Inhibition of proliferative responses of mouse spleen lymphocytes by lacto- and ovotransferrins. Food and Agricultural Immunology 1997, 9:193-201.
    • (1997) Food and Agricultural Immunology , vol.9 , pp. 193-201
    • Otani, H.1    Odashima, M.2
  • 67
    • 0034826933 scopus 로고    scopus 로고
    • Identification of choroidal ovotransferrin as a potential ocular growth regulator
    • Rada J.A., Huang Y., Rada K.G. Identification of choroidal ovotransferrin as a potential ocular growth regulator. Current Eye Research 2001, 22:121-132.
    • (2001) Current Eye Research , vol.22 , pp. 121-132
    • Rada, J.A.1    Huang, Y.2    Rada, K.G.3
  • 69
    • 0001730934 scopus 로고
    • Analysis, fractionation, and purification of egg white proteins with cellulose-cation exchanger
    • Rhodes M., Azari P., Feeney R. Analysis, fractionation, and purification of egg white proteins with cellulose-cation exchanger. The Journal of Biological Chemistry 1958, 230:399-408.
    • (1958) The Journal of Biological Chemistry , vol.230 , pp. 399-408
    • Rhodes, M.1    Azari, P.2    Feeney, R.3
  • 70
    • 0002496077 scopus 로고
    • Raw hen egg white and the role of iron in growth inhibition of Shigella dysenteriae, Staphylococcus aureus, Escherichia coli and Saccharomyces cerevisiae
    • Schade A.L., Caroline L. Raw hen egg white and the role of iron in growth inhibition of Shigella dysenteriae, Staphylococcus aureus, Escherichia coli and Saccharomyces cerevisiae. Science 1944, 100:14-15.
    • (1944) Science , vol.100 , pp. 14-15
    • Schade, A.L.1    Caroline, L.2
  • 71
    • 69549095700 scopus 로고    scopus 로고
    • Antimicrobial effect of kappa-carrageenan-based edible film containing ovotransferrin in fresh chicken breast stored at 5°C
    • Seol K.-H., Lim D.-G., Jang A., Jo C., Lee M. Antimicrobial effect of kappa-carrageenan-based edible film containing ovotransferrin in fresh chicken breast stored at 5°C. Meat Science 2009, 83:479-483.
    • (2009) Meat Science , vol.83 , pp. 479-483
    • Seol, K.-H.1    Lim, D.-G.2    Jang, A.3    Jo, C.4    Lee, M.5
  • 72
    • 77954558977 scopus 로고    scopus 로고
    • Identification of novel antioxidative peptides derived from a thermolytic hydrolysate of ovotransferrin by LC-MS/MS
    • Shen S., Chahal B., Majumder K., You S.-J., Wu J. Identification of novel antioxidative peptides derived from a thermolytic hydrolysate of ovotransferrin by LC-MS/MS. Journal of Agricultural and Food Chemistry 2010, 58:7664-7672.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , pp. 7664-7672
    • Shen, S.1    Chahal, B.2    Majumder, K.3    You, S.-J.4    Wu, J.5
  • 75
    • 70349649363 scopus 로고    scopus 로고
    • Purification process for the preparation and characterizations of hen egg white ovalbumin, lysozyme, ovotransferrin, and ovomucoid
    • Tankrathok A., Daduang S., Patramanon R., Araki T., Thammasirirak S. Purification process for the preparation and characterizations of hen egg white ovalbumin, lysozyme, ovotransferrin, and ovomucoid. Preparative Biochemistry & Biotechnology 2009, 39:380-399.
    • (2009) Preparative Biochemistry & Biotechnology , vol.39 , pp. 380-399
    • Tankrathok, A.1    Daduang, S.2    Patramanon, R.3    Araki, T.4    Thammasirirak, S.5
  • 78
    • 0020261652 scopus 로고
    • The antimicrobial defense of avian eggs: Biological perspective and chemical basis
    • Tranter H.S., Board R.G. The antimicrobial defense of avian eggs: Biological perspective and chemical basis. Journal of Applied Biochemistry 1982, 4:295-338.
    • (1982) Journal of Applied Biochemistry , vol.4 , pp. 295-338
    • Tranter, H.S.1    Board, R.G.2
  • 79
    • 0028861499 scopus 로고
    • Isolation of hen egg white lysozyme, ovotransferrin and ovalbumin, using a quaternary ammonium bound to a highly crosslinked agarose matrix
    • Vachier M.C., Piot M., Awadé A.C. Isolation of hen egg white lysozyme, ovotransferrin and ovalbumin, using a quaternary ammonium bound to a highly crosslinked agarose matrix. Journal of Chromatography. B, Biomedical Sciences and Applications 1995, 664:201-210.
    • (1995) Journal of Chromatography. B, Biomedical Sciences and Applications , vol.664 , pp. 201-210
    • Vachier, M.C.1    Piot, M.2    Awadé, A.C.3
  • 83
    • 0018820352 scopus 로고
    • Capacity of Staphylococci to grow in the presence of ovotransferrin or CrCl3 as a character of potential pathogenicity
    • Valenti P., Stasio A., Seganti L., Mastromarino P., Sinibaldi L., Orsi N. Capacity of Staphylococci to grow in the presence of ovotransferrin or CrCl3 as a character of potential pathogenicity. Journal of Clinical Microbiology 1980, 11:445-447.
    • (1980) Journal of Clinical Microbiology , vol.11 , pp. 445-447
    • Valenti, P.1    Stasio, A.2    Seganti, L.3    Mastromarino, P.4    Sinibaldi, L.5    Orsi, N.6
  • 84
    • 0021989787 scopus 로고
    • Antifungal activity of ovotransferrin towards genus Candida
    • Valenti P., Visca P., Antonini G., Orsi N. Antifungal activity of ovotransferrin towards genus Candida. Mycopathologia 1985, 89:169-175.
    • (1985) Mycopathologia , vol.89 , pp. 169-175
    • Valenti, P.1    Visca, P.2    Antonini, G.3    Orsi, N.4
  • 85
    • 0022574292 scopus 로고
    • Interaction between lactoferrin and ovotransferrin and Candida cells
    • Valenti P., Visca P., Antonini G., Orsi N. Interaction between lactoferrin and ovotransferrin and Candida cells. FEMS Microbiology Letters 1986, 33:271-275.
    • (1986) FEMS Microbiology Letters , vol.33 , pp. 271-275
    • Valenti, P.1    Visca, P.2    Antonini, G.3    Orsi, N.4
  • 90
    • 0014298819 scopus 로고
    • A comparison of glycopeptides from the ovotransferrin and serum transferrin of the hen
    • Williams J. A comparison of glycopeptides from the ovotransferrin and serum transferrin of the hen. Biochemistry Journal 1968, 108:57-67.
    • (1968) Biochemistry Journal , vol.108 , pp. 57-67
    • Williams, J.1
  • 92
    • 0018092708 scopus 로고
    • The iron-binding properties of hen ovotransferrin
    • Williams J., Evans R., Moreton K. The iron-binding properties of hen ovotransferrin. Biochemistry Journal 1978, 173:535-542.
    • (1978) Biochemistry Journal , vol.173 , pp. 535-542
    • Williams, J.1    Evans, R.2    Moreton, K.3
  • 93
    • 0021881018 scopus 로고
    • Selective reduction of a disulphide bridge in hen ovotransferrin
    • Williams J., Moreton K., Goodearl A.D.J. Selective reduction of a disulphide bridge in hen ovotransferrin. Biochemistry Journal 1985, 228:661-665.
    • (1985) Biochemistry Journal , vol.228 , pp. 661-665
    • Williams, J.1    Moreton, K.2    Goodearl, A.D.J.3
  • 94
    • 0036355060 scopus 로고    scopus 로고
    • Identification of ovotransferrin as an acute phase protein in chickens
    • Xie H., Huff G.R., Huff W.E., Balog J.M., Holt P., Rath N.C. Identification of ovotransferrin as an acute phase protein in chickens. Poultry Science 2002, 81:112-120.
    • (2002) Poultry Science , vol.81 , pp. 112-120
    • Xie, H.1    Huff, G.R.2    Huff, W.E.3    Balog, J.M.4    Holt, P.5    Rath, N.C.6
  • 96
    • 0036006230 scopus 로고    scopus 로고
    • Changes in serum ovotransferrin levels in chickens with experimentally induced inflammation and diseases
    • Xie H., Newberry L., Clark F.D., Huff W.E., Huff G.R., Balog J.M., et al. Changes in serum ovotransferrin levels in chickens with experimentally induced inflammation and diseases. Avian Diseases 2002, 46:122-131.
    • (2002) Avian Diseases , vol.46 , pp. 122-131
    • Xie, H.1    Newberry, L.2    Clark, F.D.3    Huff, W.E.4    Huff, G.R.5    Balog, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.