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Volumn 6, Issue 2, 1996, Pages 129-145

Purification and characterization of lactoferrin, lactoperoxidase, lysozyme and immunoglobulins from camel's milk

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE; CAMELIDAE; VISCUM ALBUM;

EID: 0030455418     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/0958-6946(94)00055-7     Document Type: Article
Times cited : (87)

References (32)
  • 1
    • 0013893538 scopus 로고
    • Lactoperoxidase VI. Immunochemical studies on lactoperoxidase from the milk on several species
    • Allen, P. Z. & Morrison, M. (1966). Lactoperoxidase VI. Immunochemical studies on lactoperoxidase from the milk on several species. Arch. Biochem. Biophys., 113, 540-547.
    • (1966) Arch. Biochem. Biophys. , vol.113 , pp. 540-547
    • Allen, P.Z.1    Morrison, M.2
  • 3
    • 0001755293 scopus 로고
    • Inhibition of pathogenic bacteria by camel's milk: Relation to whey lysozyme and stage of lactation
    • Barbour, E. K., Nabbut, N. H., Frerichs, W. M. & Al-Nakhli, H. M. (1984). Inhibition of pathogenic bacteria by camel's milk: relation to whey lysozyme and stage of lactation. J. Food prot. 47, 838-840.
    • (1984) J. Food Prot. , vol.47 , pp. 838-840
    • Barbour, E.K.1    Nabbut, N.H.2    Frerichs, W.M.3    Al-Nakhli, H.M.4
  • 4
    • 0015243901 scopus 로고
    • Physicochemical and immunochemical studies of bovine IgA and glycoprotein-A
    • Butler, J. E. (1971). Physicochemical and immunochemical studies of bovine IgA and glycoprotein-A. Biochim. Biophys. Acta, 251, 435-449.
    • (1971) Biochim. Biophys. Acta , vol.251 , pp. 435-449
    • Butler, J.E.1
  • 7
    • 0021733059 scopus 로고
    • Isolation and purification of bovine immunoglobulins: Use of sephacryl S-300 filtration avoids protein precipitation steps
    • Collard, A., Pivvon, P., Portetelle, D., Gregoire, R. & Burny, A. (1984). Isolation and purification of bovine immunoglobulins: use of sephacryl S-300 filtration avoids protein precipitation steps. Ann. Vet. Res., 15, 497-501.
    • (1984) Ann. Vet. Res. , vol.15 , pp. 497-501
    • Collard, A.1    Pivvon, P.2    Portetelle, D.3    Gregoire, R.4    Burny, A.5
  • 8
    • 0024218969 scopus 로고
    • Purification of camel milk lysozyme and its lytic effect on Escherichia coli and Micrococcus lysodeikticus
    • Duhaiman, A. S. (1988). Purification of camel milk lysozyme and its lytic effect on Escherichia coli and Micrococcus lysodeikticus. Comp. Biochem. Physiol., 91B, 793-796.
    • (1988) Comp. Biochem. Physiol. , vol.91 B , pp. 793-796
    • Duhaiman, A.S.1
  • 10
    • 0022501245 scopus 로고
    • Fast protein liquid chromatography of antibacterial components in milk, lactoperoxidase, lactoferrin and lysozyme
    • Ekstrand, B. & Bjorck, L. (1986). Fast protein liquid chromatography of antibacterial components in milk, lactoperoxidase, lactoferrin and lysozyme. J. Chromatogr., 358, 429-433.
    • (1986) J. Chromatogr. , vol.358 , pp. 429-433
    • Ekstrand, B.1    Bjorck, L.2
  • 11
    • 0026859989 scopus 로고
    • Antibacterial and antiviral activity of camel milk protective proteins
    • Elagamy, E. I., Ruppanner, R., Ismail, A., Champagne, C. P. & Assaf, R. (1992). Antibacterial and antiviral activity of camel milk protective proteins. J. Dairy Res. 59, 169-175.
    • (1992) J. Dairy Res. , vol.59 , pp. 169-175
    • Elagamy, E.I.1    Ruppanner, R.2    Ismail, A.3    Champagne, C.P.4    Assaf, R.5
  • 12
    • 0017990368 scopus 로고
    • 2b immunoglobulins from mouse serum using protein-A sepharose
    • 2b immunoglobulins from mouse serum using protein-A sepharose. Immunochemistry, 15, 429-436.
    • (1978) Immunochemistry , vol.15 , pp. 429-436
    • Ey, P.L.1    Prose, S.J.2    Jenkin, C.R.3
  • 15
    • 0014573323 scopus 로고
    • The demonstration of two γ-globulin subclasses in the goat
    • Gray, G. D., Nickelson, M. M. & Crim, J. A. (1969). The demonstration of two γ-globulin subclasses in the goat. Immunochemistry, 6, 641-644.
    • (1969) Immunochemistry , vol.6 , pp. 641-644
    • Gray, G.D.1    Nickelson, M.M.2    Crim, J.A.3
  • 17
    • 0015550568 scopus 로고
    • Determination of the optimal ammonium sulfate concentration for the fractionation of rabbit, sheep, horse and goat antisera
    • Hebert, G. A., Pelham, P. L. & Pittman, B. (1973). Determination of the optimal ammonium sulfate concentration for the fractionation of rabbit, sheep, horse and goat antisera. Appl. Microbiol., 25, 26-36.
    • (1973) Appl. Microbiol. , vol.25 , pp. 26-36
    • Hebert, G.A.1    Pelham, P.L.2    Pittman, B.3
  • 19
    • 0004041235 scopus 로고
    • Blackwell Scientific Publication Co., London, U.K.
    • Johnstone, A. and Thorpe, R. (1985). Immunochemistry in Practice. Blackwell Scientific Publication Co., London, U.K. pp. 27-30.
    • (1985) Immunochemistry in Practice , pp. 27-30
    • Johnstone, A.1    Thorpe, R.2
  • 20
    • 0024595854 scopus 로고
    • Interaction of lactoperoxidase with hydrogen peroxide: Formation of enzyme intermediates and generation of free radicals
    • Kohler, H. & Jenzer, H. (1989). Interaction of lactoperoxidase with hydrogen peroxide: formation of enzyme intermediates and generation of free radicals. Free Radical Biol. Med., 6, 323-339.
    • (1989) Free Radical Biol. Med. , vol.6 , pp. 323-339
    • Kohler, H.1    Jenzer, H.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0022461022 scopus 로고
    • Improved agar plate assays of bovine lysozyme and haemolytic complement activity
    • Lie, O., Syed, M. & Solbu, H. (1986). Improved agar plate assays of bovine lysozyme and haemolytic complement activity. Acta Vet. Scand., 27, 23-32.
    • (1986) Acta Vet. Scand. , vol.27 , pp. 23-32
    • Lie, O.1    Syed, M.2    Solbu, H.3
  • 23
    • 0020608467 scopus 로고
    • Antibacterial properties of milk: IgA-peroxidase-lactoferrin interactions
    • The Secretory Immune system, J. R. McGhee & J. Mestecky eds
    • Moldoveanu, Z., Tenovuo, J., Pruitt, K. M., Mansson-Rahemtulla, B. & Mestecky, J. (1983). Antibacterial properties of milk: IgA-peroxidase-lactoferrin interactions. The Secretory Immune system, J. R. McGhee & J. Mestecky eds, Annals of the New York Academy of Sciences, 409, 848-850.
    • (1983) Annals of the New York Academy of Sciences , vol.409 , pp. 848-850
    • Moldoveanu, Z.1    Tenovuo, J.2    Pruitt, K.M.3    Mansson-Rahemtulla, B.4    Mestecky, J.5
  • 24
    • 0039857288 scopus 로고
    • Lactoperoxidase II. Isolation
    • Morrison, M. & Hultquist, D. E. (1963). Lactoperoxidase II. Isolation. J. Biol. Chem., 238, 2847-2849.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2847-2849
    • Morrison, M.1    Hultquist, D.E.2
  • 25
    • 0015031923 scopus 로고
    • Isolation and characterization of IgM from bovine colostral whey
    • Mukkur, T. K. S. & Froese, A. (1971). Isolation and characterization of IgM from bovine colostral whey. Immunochemistry, 8, 257-264.
    • (1971) Immunochemistry , vol.8 , pp. 257-264
    • Mukkur, T.K.S.1    Froese, A.2
  • 27
    • 0016830865 scopus 로고
    • Steady-state kinetics of lactoperoxidase with ABTS as chromogen
    • Shindler, J. S. & Bardsley, W. G. (1975). Steady-state kinetics of lactoperoxidase with ABTS as chromogen. Biochem. Biophys. Res. Commun., 67, 1307-1312.
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 1307-1312
    • Shindler, J.S.1    Bardsley, W.G.2
  • 28
    • 0017185397 scopus 로고
    • Characterization of porcine serum immunoglobulins IgG, IgM, IgA and the preparation of mono-specific antichain sera
    • Setcavage, T. M. & Kim, Y. B. (1976). Characterization of porcine serum immunoglobulins IgG, IgM, IgA and the preparation of mono-specific antichain sera. Immunochemistry, 13, 643-652.
    • (1976) Immunochemistry , vol.13 , pp. 643-652
    • Setcavage, T.M.1    Kim, Y.B.2
  • 29
    • 85010248494 scopus 로고
    • Susceptibility of several microorganisms to milk lysozymes
    • Vakil, J. R., Chandan, R. C., Parry, R. M. & Shahani, K. M. (1969). Susceptibility of several microorganisms to milk lysozymes. J. Dairy Sci. 52, 1192-1197.
    • (1969) J. Dairy Sci. , vol.52 , pp. 1192-1197
    • Vakil, J.R.1    Chandan, R.C.2    Parry, R.M.3    Shahani, K.M.4
  • 30
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecylsulfate polyacrylamide gel electrophoresis
    • Weber, K. & Osborn, M. (1969). The reliability of molecular weight determinations by dodecylsulfate polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4405-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4405-4412
    • Weber, K.1    Osborn, M.2
  • 31
    • 0011347179 scopus 로고
    • Isolation of lactoperoxidase of 89,000 daltons and a globulin of 81,000 daltons from milk acid whey
    • Yoshida, S. (1988). Isolation of lactoperoxidase of 89,000 daltons and a globulin of 81,000 daltons from milk acid whey. J. Dairy Sci. 71, 2021-2027.
    • (1988) J. Dairy Sci. , vol.71 , pp. 2021-2027
    • Yoshida, S.1
  • 32
    • 0000282103 scopus 로고
    • Isolation of lactoperoxidase and lactoferrin from bovine milk rennet whey and acid whey by sulphopropyl cation-exchange chromatography
    • Yoshida, S. & Ye-Xiuyun (1991). Isolation of lactoperoxidase and lactoferrin from bovine milk rennet whey and acid whey by sulphopropyl cation-exchange chromatography. Neth. Milk and Dairy J. 45, 273-280.
    • (1991) Neth. Milk and Dairy J. , vol.45 , pp. 273-280
    • Yoshida, S.1    Ye-Xiuyun2


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