메뉴 건너뛰기




Volumn 21, Issue 9, 2010, Pages 455-463

Ovomucin - a glycoprotein with promising potential

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-BACTERIAL; ANTI-TUMORS; BIOLOGICAL PROPERTIES; EGG WHITE; EGG WHITE PROTEINS; FUNCTIONAL FOODS; NEW APPLICATIONS; NUTRACEUTICALS;

EID: 77956616427     PISSN: 09242244     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tifs.2010.07.001     Document Type: Review
Times cited : (103)

References (84)
  • 1
    • 0015887485 scopus 로고
    • Solubilization and characterization of ovomucin without chemical modification
    • Adachi N., Azuma J., Janado M., Onodera K. Solubilization and characterization of ovomucin without chemical modification. Agricultural and Biological Chemistry 1973, 37(9):2175-2180.
    • (1973) Agricultural and Biological Chemistry , vol.37 , Issue.9 , pp. 2175-2180
    • Adachi, N.1    Azuma, J.2    Janado, M.3    Onodera, K.4
  • 2
    • 0033050814 scopus 로고    scopus 로고
    • Comparison of three liquid chromatographic methods for egg-white protein analysis
    • Awade A.C., Efstathiou T. Comparison of three liquid chromatographic methods for egg-white protein analysis. Journal of Chromatography B 1999, 723:69-74.
    • (1999) Journal of Chromatography B , vol.723 , pp. 69-74
    • Awade, A.C.1    Efstathiou, T.2
  • 3
    • 0028023255 scopus 로고
    • Two-step chromatographic procedures for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins
    • Awade A.C., Moreau S., Molle D., Brule G., Maubois J.L. Two-step chromatographic procedures 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
    • Awade, A.C.1    Moreau, S.2    Molle, D.3    Brule, G.4    Maubois, J.L.5
  • 4
    • 0009030827 scopus 로고
    • Thinning of thick albumen in shell eggs - changes in ovomucin
    • Baliga B.R., Kadkol S.B., Lahiry N.L. Thinning of thick albumen in shell eggs - changes in ovomucin. Poultry Science 1971, 50(2):466-473.
    • (1971) Poultry Science , vol.50 , Issue.2 , pp. 466-473
    • Baliga, B.R.1    Kadkol, S.B.2    Lahiry, N.L.3
  • 5
    • 0030972842 scopus 로고    scopus 로고
    • Foaming properties of egg albumen with a bubbling apparatus compared with whipping
    • Baniel A., Fains A., Popineau Y. Foaming properties of egg albumen with a bubbling apparatus compared with whipping. Journal of Food Science 1997, 62:377-381.
    • (1997) Journal of Food Science , vol.62 , pp. 377-381
    • Baniel, A.1    Fains, A.2    Popineau, Y.3
  • 6
    • 84987311643 scopus 로고
    • Effects of sulphydryl blocking on the thinning of egg white
    • Beveridge T., Nakai S. Effects of sulphydryl blocking on the thinning of egg white. Journal of Food Science 1975, 40:864-868.
    • (1975) Journal of Food Science , vol.40 , pp. 864-868
    • Beveridge, T.1    Nakai, S.2
  • 7
    • 0001517098 scopus 로고
    • The mechanical properties of the thick white of the hen's egg
    • Brooks J., Hale H.P. The mechanical properties of the thick white of the hen's egg. Biochimica et Biophysica Acta 1959, 32:237-250.
    • (1959) Biochimica et Biophysica Acta , vol.32 , pp. 237-250
    • Brooks, J.1    Hale, H.P.2
  • 8
    • 0009083693 scopus 로고
    • The mechanical properties of the thick white of the hen's egg. II. The relation between rigidity and composition
    • Brooks J., Hale H.P. The mechanical properties of the thick white of the hen's egg. II. The relation between rigidity and composition. Biochimica et Biophysica Acta 1961, 46:289-301.
    • (1961) Biochimica et Biophysica Acta , vol.46 , pp. 289-301
    • Brooks, J.1    Hale, H.P.2
  • 9
    • 0002095708 scopus 로고
    • The albumen: chemistry
    • John Wiley and Sons, New York, R.W. Burley, D.V. Vadehra (Eds.)
    • Burley R.W., Vadehra D.V. The albumen: chemistry. The avian egg: Chemistry and biology 1989, 65-128. John Wiley and Sons, New York. R.W. Burley, D.V. Vadehra (Eds.).
    • (1989) The avian egg: Chemistry and biology , pp. 65-128
    • Burley, R.W.1    Vadehra, D.V.2
  • 11
    • 0042472687 scopus 로고
    • Egg white lysozyme. 3. The effect of pH on the lysozyme - ovomucin interaction
    • Cotterill O.J., Winter A.R. Egg white lysozyme. 3. The effect of pH on the lysozyme - ovomucin interaction. Poultry Science 1955, 34:679-687.
    • (1955) Poultry Science , vol.34 , pp. 679-687
    • Cotterill, O.J.1    Winter, A.R.2
  • 12
    • 0014965882 scopus 로고
    • Chemical and physical characterization of ovomucin, a sulfated glycoprotein complex from chicken eggs
    • Donovan J.W., Davis J.G., White L.M. Chemical and physical characterization of ovomucin, a sulfated glycoprotein complex from chicken eggs. Biochimica et Biophysica Acta 1970, 207:190-201.
    • (1970) Biochimica et Biophysica Acta , vol.207 , pp. 190-201
    • Donovan, J.W.1    Davis, J.G.2    White, L.M.3
  • 14
  • 16
    • 0017875967 scopus 로고
    • Mucin-type glycoproteins; new perspectives on their structure and synthesis
    • Gallagher J.T., Corfield A.P. Mucin-type glycoproteins; new perspectives on their structure and synthesis. Trends in Biochemical Sciences 1978, 3:38-41.
    • (1978) Trends in Biochemical Sciences , vol.3 , pp. 38-41
    • Gallagher, J.T.1    Corfield, A.P.2
  • 17
    • 0346744769 scopus 로고
    • Product of interaction between influenza virus enzyme and ovomucin
    • Gottschalk A., Lind P. Product of interaction between influenza virus enzyme and ovomucin. Nature 1949, 164:232-233.
    • (1949) Nature , vol.164 , pp. 232-233
    • Gottschalk, A.1    Lind, P.2
  • 18
    • 70349680685 scopus 로고
    • Sulfhydryl groups in proteins - II. Edestin, excelsin and globin in solutions of guanidine hydrochloride, urea and their derivatives
    • Greenstein J.P. Sulfhydryl groups in proteins - II. Edestin, excelsin and globin in solutions of guanidine hydrochloride, urea and their derivatives. Journal of Biological Chemistry 1939, 128(1):233-240.
    • (1939) Journal of Biological Chemistry , vol.128 , Issue.1 , pp. 233-240
    • Greenstein, J.P.1
  • 19
    • 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
  • 20
    • 44349121133 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of ovomucin and effect on foaming properties
    • Hammershoj M., Nebel C.C., Carstens J.H. Enzymatic hydrolysis of ovomucin and effect on foaming properties. Food Research International 2008, 41(5):522-531.
    • (2008) Food Research International , vol.41 , Issue.5 , pp. 522-531
    • Hammershoj, M.1    Nebel, C.C.2    Carstens, J.H.3
  • 21
    • 0347708738 scopus 로고    scopus 로고
    • Importance of hen age and egg storage time for egg albumen foaming
    • Hammershoj M., Qvist K.B. Importance of hen age and egg storage time for egg albumen foaming. Lebensmittel-Wissenschaft Und-Technologie 2001, 34(2):118-120.
    • (2001) Lebensmittel-Wissenschaft Und-Technologie , vol.34 , Issue.2 , pp. 118-120
    • Hammershoj, M.1    Qvist, K.B.2
  • 23
    • 0010101538 scopus 로고
    • The action of egg white lysozyme on ovomucoid and ovomucin
    • Hawthorne J.R. The action of egg white lysozyme on ovomucoid and ovomucin. Biochimica et Biophysica Acta 1950, 6:28-35.
    • (1950) Biochimica et Biophysica Acta , vol.6 , pp. 28-35
    • Hawthorne, J.R.1
  • 24
    • 0017051299 scopus 로고
    • Studies on the dissociation of the soluble ovomucin by sonication
    • Hayakawa S., Sato Y. Studies on the dissociation of the soluble ovomucin by sonication. Agricultural and Biological Chemistry 1976, 40:2397-2404.
    • (1976) Agricultural and Biological Chemistry , vol.40 , pp. 2397-2404
    • Hayakawa, S.1    Sato, Y.2
  • 25
    • 84900962519 scopus 로고    scopus 로고
    • Ovomucin
    • Springer Verlag, Germany, R. Huopalahti, R. Lopez-Fandino, M. Anton, R. Schade (Eds.)
    • Hiidenhovi J. Ovomucin. Bioactive egg compounds 2007, 61-68. Springer Verlag, Germany. R. Huopalahti, R. Lopez-Fandino, M. Anton, R. Schade (Eds.).
    • (2007) Bioactive egg compounds , pp. 61-68
    • Hiidenhovi, J.1
  • 26
    • 0032940323 scopus 로고    scopus 로고
    • Separation of ovomucin subunits by gel filtration: enhanced resolution of subunits by using dual-column system
    • Hiidenhovi J., Aro H.S., Kankare V. Separation of ovomucin subunits by gel filtration: enhanced resolution of subunits by using dual-column system. Journal of Agricultural and Food Chemistry 1999, 47:1004-1008.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 1004-1008
    • Hiidenhovi, J.1    Aro, H.S.2    Kankare, V.3
  • 27
    • 44349125901 scopus 로고    scopus 로고
    • Ovomucin purification: some preliminary studies to modify the isoelectric precipitation method
    • ISPAIA, Saint-Brieuc, France, Y. Nys (Ed.)
    • Hiidenhovi J., Huopalahti R., Ryhänen E.L. Ovomucin purification: some preliminary studies to modify the isoelectric precipitation method. Quality of eggs and egg products 2003, 388-394. ISPAIA, Saint-Brieuc, France. Y. Nys (Ed.).
    • (2003) Quality of eggs and egg products , pp. 388-394
    • Hiidenhovi, J.1    Huopalahti, R.2    Ryhänen, E.L.3
  • 29
    • 84987299322 scopus 로고
    • Studies on the characterization of ovomucin and chalaza of the hen's egg
    • Itoh T., Miyazaki J., Sugawara H., Adachi A. Studies on the characterization of ovomucin and chalaza of the hen's egg. Journal of Food Science 1987, 52:1518-1521.
    • (1987) Journal of Food Science , vol.52 , pp. 1518-1521
    • Itoh, T.1    Miyazaki, J.2    Sugawara, H.3    Adachi, A.4
  • 30
    • 84985287183 scopus 로고
    • Egg albumen proteins interactions in an angel food cake system
    • Johnson T.M., Zabik M.E. Egg albumen proteins interactions in an angel food cake system. Journal of Food Science 1981, 46:1231-1236.
    • (1981) Journal of Food Science , vol.46 , pp. 1231-1236
    • Johnson, T.M.1    Zabik, M.E.2
  • 31
    • 0015765990 scopus 로고
    • Nature of the carbohydrate side chains and their linkage to the protein in chicken egg white ovomucin
    • Kato A., Fujinaga K., Yagishita K. Nature of the carbohydrate side chains and their linkage to the protein in chicken egg white ovomucin. Agricultural and Biological Chemistry 1973, 37:2479-2485.
    • (1973) Agricultural and Biological Chemistry , vol.37 , pp. 2479-2485
    • Kato, A.1    Fujinaga, K.2    Yagishita, K.3
  • 33
    • 0000230525 scopus 로고
    • Studies on changes in stored shell eggs. Part VI. Changes in the chemical composition of ovomucin during storage
    • Kato A., Nakamura R., Sato Y. Studies on changes in stored shell eggs. Part VI. Changes in the chemical composition of ovomucin during storage. Agricultural and Biological Chemistry 1970, 34:1009-1013.
    • (1970) Agricultural and Biological Chemistry , vol.34 , pp. 1009-1013
    • Kato, A.1    Nakamura, R.2    Sato, Y.3
  • 34
    • 0344732458 scopus 로고
    • Studies on changes in stored shell eggs part VII. Changes in the physicochemical properties of ovomucin solubilized by treatment with mercaptoethanol during storage
    • Kato A., Nakamura R., Sato Y. Studies on changes in stored shell eggs part VII. Changes in the physicochemical properties of ovomucin solubilized by treatment with mercaptoethanol during storage. Agricultural and Biological Chemistry 1971, 35:351-356.
    • (1971) Agricultural and Biological Chemistry , vol.35 , pp. 351-356
    • Kato, A.1    Nakamura, R.2    Sato, Y.3
  • 37
    • 0017758902 scopus 로고
    • Separation of ovomucin into carbohydrate rich and poor components by chromatography on lysozyme-sepharose 4B
    • Kato A., Ogino K., Matsudomi N., Kobayashi K. Separation of ovomucin into carbohydrate rich and poor components by chromatography on lysozyme-sepharose 4B. Agricultural and Biological Chemistry 1977, 41:1925-1929.
    • (1977) Agricultural and Biological Chemistry , vol.41 , pp. 1925-1929
    • Kato, A.1    Ogino, K.2    Matsudomi, N.3    Kobayashi, K.4
  • 38
    • 0002765706 scopus 로고
    • Changes in the emulsifying and foaming properties of proteins during heat denaturation
    • Kato A., Osako Y., Matsudomi N., Kobayashi K. Changes in the emulsifying and foaming properties of proteins during heat denaturation. Agricultural and Biological Chemistry 1983, 47(1):33-37.
    • (1983) Agricultural and Biological Chemistry , vol.47 , Issue.1 , pp. 33-37
    • Kato, A.1    Osako, Y.2    Matsudomi, N.3    Kobayashi, K.4
  • 39
    • 85008543442 scopus 로고
    • The separation and characterization of carbohydrate rich component from ovomucin in chicken eggs
    • Kato A., Sato Y. The separation and characterization of carbohydrate rich component from ovomucin in chicken eggs. Agricultural and Biological Chemistry 1971, 35:439-440.
    • (1971) Agricultural and Biological Chemistry , vol.35 , pp. 439-440
    • Kato, A.1    Sato, Y.2
  • 40
    • 0242344499 scopus 로고
    • Studies on changes in stored shell eggs. VIII the release of carbohydrate rich component from ovomucin gel during storage
    • Kato A., Sato Y. Studies on changes in stored shell eggs. VIII the release of carbohydrate rich component from ovomucin gel during storage. Agricultural and Biological Chemistry 1972, 36(5):831-836.
    • (1972) Agricultural and Biological Chemistry , vol.36 , Issue.5 , pp. 831-836
    • Kato, A.1    Sato, Y.2
  • 44
    • 0030792933 scopus 로고    scopus 로고
    • Sialic acids in molecular and cellular recognition
    • Kelm S., Schauer R. Sialic acids in molecular and cellular recognition. International Reviews in Cytology 1997, 175:137-240.
    • (1997) International Reviews in Cytology , vol.175 , pp. 137-240
    • Kelm, S.1    Schauer, R.2
  • 46
    • 77956616930 scopus 로고    scopus 로고
    • Inhibitor of Helicobacter pylori colonization. US Patent, 6,235,709 B1.
    • Kodama, Y., & Kimura, N. (1999). Inhibitor of Helicobacter pylori colonization. US Patent, 6,235,709 B1.
    • (1999)
    • Kodama, Y.1    Kimura, N.2
  • 47
    • 0642272907 scopus 로고
    • The egg white inhibitor of influenza virus hemagglutination. I. Preparation and properties of semipurified inhibitor
    • Lanni F., Sharp D.G., Eckert E.A., Dillon E.S., Beard D., Beard J.W. The egg white inhibitor of influenza virus hemagglutination. I. Preparation and properties of semipurified inhibitor. The Journal of Biological Chemistry 1949, 179:1275-1287.
    • (1949) The Journal of Biological Chemistry , vol.179 , pp. 1275-1287
    • Lanni, F.1    Sharp, D.G.2    Eckert, E.A.3    Dillon, E.S.4    Beard, D.5    Beard, J.W.6
  • 49
    • 0346586199 scopus 로고
    • Chemistry of shell egg deterioration: effect of reducing agents
    • Mac-Donnell L.R., Lineweaver H., Feeney R.E. Chemistry of shell egg deterioration: effect of reducing agents. Poultry Science 1951, 30:856-863.
    • (1951) Poultry Science , vol.30 , pp. 856-863
    • Mac-Donnell, L.R.1    Lineweaver, H.2    Feeney, R.E.3
  • 50
    • 0028873168 scopus 로고
    • Recent advances in the understanding of egg white protein functionality
    • Mine Y. Recent advances in the understanding of egg white protein functionality. Trends in Food Science & Technology 1995, 6:225-232.
    • (1995) Trends in Food Science & Technology , vol.6 , pp. 225-232
    • Mine, Y.1
  • 51
    • 33645501006 scopus 로고    scopus 로고
    • New insights in biologically active proteins and peptides derived from hen egg
    • Mine Y., Kovacs-Nolan J. New insights in biologically active proteins and peptides derived from hen egg. World's Poultry Science Journal 2006, 62(1):87-95.
    • (2006) World's Poultry Science Journal , vol.62 , Issue.1 , pp. 87-95
    • Mine, Y.1    Kovacs-Nolan, J.2
  • 52
    • 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., Watanabe K. Egg ovomucin attenuates hypercholesterolemia in rats and inhibits cholesterol absorption in Caco-2 cells. Lipids 2002, 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
  • 53
    • 84885514205 scopus 로고
    • Studies on the foaming property of chicken egg white. X. On the role of ovomucin (B) in egg white foaminess (The mechanism of foaminess (2))
    • Nakamura R., Sato Y. Studies on the foaming property of chicken egg white. X. On the role of ovomucin (B) in egg white foaminess (The mechanism of foaminess (2)). Agricultural and Biological Chemistry 1964, 28:530-534.
    • (1964) Agricultural and Biological Chemistry , vol.28 , pp. 530-534
    • Nakamura, R.1    Sato, Y.2
  • 55
    • 0346743235 scopus 로고    scopus 로고
    • Morphological observations on antitumour activities of 70 kDa fragment in α-subunit from pronase treated ovomucin in a double grafted tumor system
    • Oguro T., Watanabe K., Tani H., Ohishi H., Ebina T. Morphological observations on antitumour activities of 70 kDa fragment in α-subunit from pronase treated ovomucin in a double grafted tumor system. Food Science and Technology Research 2000, 6:179-185.
    • (2000) Food Science and Technology Research , vol.6 , pp. 179-185
    • Oguro, T.1    Watanabe, K.2    Tani, H.3    Ohishi, H.4    Ebina, T.5
  • 56
    • 0008991903 scopus 로고
    • Cytotoxic effect of sialoglycoprotein derived from avian egg white ovomucin on the cultured tumor cell
    • Ohami H., Ohishi H., Yokota T., Mori T., Watanabe K. Cytotoxic effect of sialoglycoprotein derived from avian egg white ovomucin on the cultured tumor cell. Medicine and Biology 1993, 126:19-23.
    • (1993) Medicine and Biology , vol.126 , pp. 19-23
    • Ohami, H.1    Ohishi, H.2    Yokota, T.3    Mori, T.4    Watanabe, K.5
  • 57
    • 66149145936 scopus 로고    scopus 로고
    • A new method of separating ovomucin from egg white
    • Omana D.A., Wu J. A new method of separating ovomucin from egg white. Journal of Agricultural and Food Chemistry 2009, 57(9):3596-3603.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , Issue.9 , pp. 3596-3603
    • Omana, D.A.1    Wu, J.2
  • 58
    • 70349743733 scopus 로고    scopus 로고
    • Effect of different concentrations of calcium chloride and potassium chloride on egg white proteins during isoelectric precipitation of ovomucin
    • Omana D.A., Wu J. Effect of different concentrations of calcium chloride and potassium chloride on egg white proteins during isoelectric precipitation of ovomucin. Poultry Science 2009, 88:2224-2234.
    • (2009) Poultry Science , vol.88 , pp. 2224-2234
    • Omana, D.A.1    Wu, J.2
  • 59
    • 43949147696 scopus 로고
    • Effects of hen egg proteins on proliferative responses of mouse spleen lymphocytes
    • Otani H., Maenishi K. Effects of hen egg proteins on proliferative responses of mouse spleen lymphocytes. Lebensmittel Wissenschaft Und Technologie 1994, 27:42-47.
    • (1994) Lebensmittel Wissenschaft Und Technologie , vol.27 , pp. 42-47
    • Otani, H.1    Maenishi, K.2
  • 60
    • 0002691911 scopus 로고
    • Principles of foam stability
    • Elsevier Applied Science, London, E. Dickinson, G. Stainsby (Eds.)
    • Prins A. Principles of foam stability. Advances in food emulsions and foams 1988, 91-121. Elsevier Applied Science, London. E. Dickinson, G. Stainsby (Eds.).
    • (1988) Advances in food emulsions and foams , pp. 91-121
    • Prins, A.1
  • 61
    • 33749628737 scopus 로고
    • Egg white glycoproteins and the physical properties of egg white
    • British Poultry Science Ltd, Edinburgh, B.M. Freeman, P.E. Lake (Eds.)
    • Robinson D.S. Egg white glycoproteins and the physical properties of egg white. Egg formation and egg production 1972, 65-86. British Poultry Science Ltd, Edinburgh. B.M. Freeman, P.E. Lake (Eds.).
    • (1972) Egg formation and egg production , pp. 65-86
    • Robinson, D.S.1
  • 62
    • 0015008596 scopus 로고
    • Studies on the composition of egg-white ovomucin
    • Robinson S.D., Monsey J.B. Studies on the composition of egg-white ovomucin. Biochemical Journal 1971, 121:537-547.
    • (1971) Biochemical Journal , vol.121 , pp. 537-547
    • Robinson, S.D.1    Monsey, J.B.2
  • 63
    • 0015265296 scopus 로고
    • Changes in the composition of ovomucin during liquefaction of thick egg white: the effect of ionic strength and magnesium salts
    • Robinson S.D., Monsey J.B. Changes in the composition of ovomucin during liquefaction of thick egg white: the effect of ionic strength and magnesium salts. Journal of the Science of Food and Agriculture 1972, 23:893-904.
    • (1972) Journal of the Science of Food and Agriculture , vol.23 , pp. 893-904
    • Robinson, S.D.1    Monsey, J.B.2
  • 64
    • 77956618409 scopus 로고    scopus 로고
    • Inactivation composition of food poisoning bacteria. Japanese Patent, 269420.
    • Ryoko, K., Makoto, H., Yukiko, K., Kazuo, K., Noriyuki, I., Tsutomu, O., & et al. (2004). Inactivation composition of food poisoning bacteria. Japanese Patent, 269420.
    • (2004)
    • Ryoko, K.1    Makoto, H.2    Yukiko, K.3    Kazuo, K.4    Noriyuki, I.5    Tsutomu, O.6
  • 65
    • 4644287980 scopus 로고    scopus 로고
    • Sialic acids: fascinating sugars in higher animals and man
    • Schauer R. Sialic acids: fascinating sugars in higher animals and man. Zoology 2004, 107:49-64.
    • (2004) Zoology , vol.107 , pp. 49-64
    • Schauer, R.1
  • 68
    • 36949070963 scopus 로고
    • Modification of ovalbumin in stored eggs detected by heat denaturation
    • Smith M.B., Back J.F. Modification of ovalbumin in stored eggs detected by heat denaturation. Nature 1962, 193:878-879.
    • (1962) Nature , vol.193 , pp. 878-879
    • Smith, M.B.1    Back, J.F.2
  • 69
    • 0001352497 scopus 로고
    • Studies on ovalbumin. 2. The formation and properties of S-ovalbumin, a more stable form
    • Smith M.B., Back J.F. Studies on ovalbumin. 2. The formation and properties of S-ovalbumin, a more stable form. Australian Journal of Biological Sciences 1965, 18:365-377.
    • (1965) Australian Journal of Biological Sciences , vol.18 , pp. 365-377
    • Smith, M.B.1    Back, J.F.2
  • 70
    • 0026612168 scopus 로고
    • 13C-NMR assignments for sialylated oligosaccharide-alditols related to mucins. Study of thirteen components from hen ovomucin and swallow nest mucin
    • 13C-NMR assignments for sialylated oligosaccharide-alditols related to mucins. Study of thirteen components from hen ovomucin and swallow nest mucin. Biochimie 1992, 74:39-52.
    • (1992) Biochimie , vol.74 , pp. 39-52
    • Strecker, G.1    Wieruszeski, J.M.2    Cuvillier, O.3    Michalski, J.C.4    Moutreuil, J.5
  • 73
    • 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., Kato A. Activation of macrophages by sulfated glycopeptides in ovomucin, yolk membrane, and chalazae in chicken eggs. Bioscience, Biotechnology and Biochemistry 1997, 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
  • 75
    • 0032871116 scopus 로고    scopus 로고
    • Ovomucin content and composition in chicken eggs with different interior quality
    • Toussant M.J., Latshaw J.D. Ovomucin content and composition in chicken eggs with different interior quality. Journal of the Science of Food and Agriculture 1999, 79:1666-1670.
    • (1999) Journal of the Science of Food and Agriculture , vol.79 , pp. 1666-1670
    • Toussant, M.J.1    Latshaw, J.D.2
  • 77
    • 0030246673 scopus 로고    scopus 로고
    • Differences in hemagglutination inhibition activity against bovine rotavirus and hen Newcastle disease virus based on the subunit in hen egg white ovomucin
    • Tsuge Y., Shimoyamada M., Watanabe K. Differences in hemagglutination inhibition activity against bovine rotavirus and hen Newcastle disease virus based on the subunit in hen egg white ovomucin. Bioscience, Biotechnology and Biochemistry 1996, 60:1505-1506.
    • (1996) Bioscience, Biotechnology and Biochemistry , vol.60 , pp. 1505-1506
    • Tsuge, Y.1    Shimoyamada, M.2    Watanabe, K.3
  • 78
    • 0001046338 scopus 로고    scopus 로고
    • Structural features of hen Newcastle disease virus and anti-ovomucin antibodies binding glycopeptides from pronase treated ovomucin
    • Tsuge Y., Shimoyamada M., Watanabe K. Structural features of hen Newcastle disease virus and anti-ovomucin antibodies binding glycopeptides from pronase treated ovomucin. Journal of Agricultural and Food Chemistry 1997, 45:2393-2398.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 2393-2398
    • Tsuge, Y.1    Shimoyamada, M.2    Watanabe, K.3
  • 79
    • 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., Watanabe K. Bindings of ovomucin to Newcastle disease virus and anti-ovomucin antibodies and its heat stability based on binding abilities. Journal of Agricultural and Food Chemistry 1997, 45:4629-4634.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 4629-4634
    • Tsuge, Y.1    Shimoyamada, M.2    Watanabe, K.3
  • 80
    • 7444235775 scopus 로고    scopus 로고
    • Amino acid sequence of a-subunit in hen egg white ovomucin deduced from cloned cDNA
    • Watanabe K., Shimoyamada M., Onizuka T., Akiyama H., Niwa M., Ido T., et al. Amino acid sequence of a-subunit in hen egg white ovomucin deduced from cloned cDNA. DNA Sequence 2004, 15(4):251-261.
    • (2004) DNA Sequence , vol.15 , Issue.4 , pp. 251-261
    • Watanabe, K.1    Shimoyamada, M.2    Onizuka, T.3    Akiyama, H.4    Niwa, M.5    Ido, T.6
  • 81
    • 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., Tsuge Y., Shimoyamada M., Ogama N., Ebina T. Antitumor effects of pronase-treated fragments, glycopeptides, from ovomucin in hen egg white in a double grafted tumor system. Journal of Agricultural and Food Chemistry 1998, 46:3033-3038.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 3033-3038
    • Watanabe, K.1    Tsuge, Y.2    Shimoyamada, M.3    Ogama, N.4    Ebina, T.5
  • 82
    • 0009031441 scopus 로고    scopus 로고
    • In vitro studies of cytotoxic effect on sarcoma-180 cells of β-subunit from egg white ovomucin
    • Yokota T., Ohishi H., Watanabe K. In vitro studies of cytotoxic effect on sarcoma-180 cells of β-subunit from egg white ovomucin. Food Science and Technology Research 1999, 5:273-278.
    • (1999) Food Science and Technology Research , vol.5 , pp. 273-278
    • Yokota, T.1    Ohishi, H.2    Watanabe, K.3
  • 83
    • 0008984399 scopus 로고    scopus 로고
    • Antitumor effects of β-subunit from egg white ovomucin on xenografted sarcoma-180 cells in mice
    • Yokota T., Ohishi H., Watanabe K. Antitumor effects of β-subunit from egg white ovomucin on xenografted sarcoma-180 cells in mice. Food Science and Technology Research 1999, 5(3):279-283.
    • (1999) Food Science and Technology Research , vol.5 , Issue.3 , pp. 279-283
    • Yokota, T.1    Ohishi, H.2    Watanabe, K.3
  • 84
    • 84987341370 scopus 로고
    • Preparation of egg white ovomucin by gel filtration
    • Young L.L., Gardner F.A. Preparation of egg white ovomucin by gel filtration. Journal of Food Science 1970, 37:8-11.
    • (1970) Journal of Food Science , vol.37 , pp. 8-11
    • Young, L.L.1    Gardner, F.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.