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Volumn 151, Issue 1, 2008, Pages 64-69

Changes in milk protein composition during acute involution at different phases of tammar wallaby (Macropus eugenii) lactation

Author keywords

Antimicrobials; Involution; Mass spectrometry; Milk composition; Tammar wallaby; Whey

Indexed keywords

BETA LACTOGLOBULIN; CARBOHYDRATE; DERMCIDIN; IMMUNOGLOBULIN RECEPTOR; LIPID; LYSOZYME; MILK PROTEIN; MONOSACCHARIDE; OLIGOSACCHARIDE; POLYMER; PROTEIN;

EID: 47949100088     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2008.05.011     Document Type: Article
Times cited : (8)

References (66)
  • 1
    • 36349007573 scopus 로고    scopus 로고
    • A proteomic approach to analysis of antimicrobial activity in marsupial pouch secretions
    • Ambatipudi K., Joss J., Raftery M., and Deane E. A proteomic approach to analysis of antimicrobial activity in marsupial pouch secretions. Dev. Comp. Immunol. 32 (2008) 108-120
    • (2008) Dev. Comp. Immunol. , vol.32 , pp. 108-120
    • Ambatipudi, K.1    Joss, J.2    Raftery, M.3    Deane, E.4
  • 2
    • 0026905387 scopus 로고
    • Collection of fore and hind milk from the sow and the changes in milk composition during suckling
    • Atwood C.S., and Hartmann P.E. Collection of fore and hind milk from the sow and the changes in milk composition during suckling. J. Dairy Res. 59 (1992) 287-298
    • (1992) J. Dairy Res. , vol.59 , pp. 287-298
    • Atwood, C.S.1    Hartmann, P.E.2
  • 5
    • 13244265550 scopus 로고    scopus 로고
    • Decharging of globular proteins and protein complexes in electrospray
    • Catalina M.I., van den Heuvel R.H., van Duijn E., and Heck A.J. Decharging of globular proteins and protein complexes in electrospray. Chemistry 11 (2005) 960-968
    • (2005) Chemistry , vol.11 , pp. 960-968
    • Catalina, M.I.1    van den Heuvel, R.H.2    van Duijn, E.3    Heck, A.J.4
  • 6
    • 0037083451 scopus 로고    scopus 로고
    • Use of proteomic methodology for the characterisation of human milk fat globular membrane proteins
    • Charlwood J., Hanrahan S., Tyldesley R., Langridge J., Dwek M., and Camilleri P. Use of proteomic methodology for the characterisation of human milk fat globular membrane proteins. Anal. Biochem. 301 (2002) 314-324
    • (2002) Anal. Biochem. , vol.301 , pp. 314-324
    • Charlwood, J.1    Hanrahan, S.2    Tyldesley, R.3    Langridge, J.4    Dwek, M.5    Camilleri, P.6
  • 7
    • 0014558453 scopus 로고
    • Mechanism of lysozyme action
    • Chipman D.M., and Sharon N. Mechanism of lysozyme action. Science 165 (1969) 454-465
    • (1969) Science , vol.165 , pp. 454-465
    • Chipman, D.M.1    Sharon, N.2
  • 9
    • 0024896419 scopus 로고
    • Lactation in the tammar wallaby (Macropus eugenii)
    • Dove H., and Cork S.J. Lactation in the tammar wallaby (Macropus eugenii). J. Zool. Lond. 219 (1989) 385-397
    • (1989) J. Zool. Lond. , vol.219 , pp. 385-397
    • Dove, H.1    Cork, S.J.2
  • 10
    • 0024234923 scopus 로고
    • Action of myeloperoxidase-hydrogen peroxide-chloride system on the egg white lysozyme
    • Drozdz R., Naskalski J.W., and Sznajd J. Action of myeloperoxidase-hydrogen peroxide-chloride system on the egg white lysozyme. Acta. Biochim. Pol. 35 (1988) 277-286
    • (1988) Acta. Biochim. Pol. , vol.35 , pp. 277-286
    • Drozdz, R.1    Naskalski, J.W.2    Sznajd, J.3
  • 11
    • 0027673058 scopus 로고
    • Can lysozymes mediate antibacterial resistance in plants?
    • During K. Can lysozymes mediate antibacterial resistance in plants?. Plant. Mol. Biol. 23 (1993) 209-214
    • (1993) Plant. Mol. Biol. , vol.23 , pp. 209-214
    • During, K.1
  • 13
    • 0026095436 scopus 로고
    • Killing of gram-negative bacteria by lactoferrin and lysozyme
    • Ellison R.T., and Giehl T.J. Killing of gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest. 88 (1991) 1080-1091
    • (1991) J. Clin. Invest. , vol.88 , pp. 1080-1091
    • Ellison, R.T.1    Giehl, T.J.2
  • 14
    • 0014227367 scopus 로고
    • Lysozyme: antigen, enzyme and antibacterial agent
    • 1968
    • Glynn A.A. Lysozyme: antigen, enzyme and antibacterial agent. Sci. Basis Med. Annu. Rev. (1968) 31-52 1968
    • (1968) Sci. Basis Med. Annu. Rev. , pp. 31-52
    • Glynn, A.A.1
  • 15
    • 0003048947 scopus 로고
    • The composition of Marsupial Milk
    • Tyndale-Biscoe C.H., and Janssens P.A. (Eds), Springer-Verlag, Heidelberg
    • Green B., and Merchant J. The composition of Marsupial Milk. In: Tyndale-Biscoe C.H., and Janssens P.A. (Eds). The Developing Marsupial: Models for Biomedical Research (1988), Springer-Verlag, Heidelberg 41-54
    • (1988) The Developing Marsupial: Models for Biomedical Research , pp. 41-54
    • Green, B.1    Merchant, J.2
  • 16
    • 0017802003 scopus 로고
    • Changes in the composition of the mammary secretion of women after abrupt termination of breast feeding
    • Hartmann P.E., and Kulski J.K. Changes in the composition of the mammary secretion of women after abrupt termination of breast feeding. J. Physiol. 275 (1978) 1-11
    • (1978) J. Physiol. , vol.275 , pp. 1-11
    • Hartmann, P.E.1    Kulski, J.K.2
  • 17
    • 0022730412 scopus 로고
    • β-lactoglobulin and α-lactalbumin in mammary secretions during the dry period: parallelism of concentration changes
    • Hurley W.L., and Rejman J.J. β-lactoglobulin and α-lactalbumin in mammary secretions during the dry period: parallelism of concentration changes. J. Dairy Sci. 69 (1985) 1642-1647
    • (1985) J. Dairy Sci. , vol.69 , pp. 1642-1647
    • Hurley, W.L.1    Rejman, J.J.2
  • 18
    • 0023062798 scopus 로고
    • Mammary function during the mature-virgin period: enzyme, lactose, protein concentrations and pH of mammary secretions
    • Hurley W.L. Mammary function during the mature-virgin period: enzyme, lactose, protein concentrations and pH of mammary secretions. J. Dairy Sci. 70 (1987) 20-28
    • (1987) J. Dairy Sci. , vol.70 , pp. 20-28
    • Hurley, W.L.1
  • 19
    • 0024675579 scopus 로고
    • Mammary gland function during involution
    • Hurley W.L. Mammary gland function during involution. J. Dairy Sci. 72 (1989) 1637-1646
    • (1989) J. Dairy Sci. , vol.72 , pp. 1637-1646
    • Hurley, W.L.1
  • 20
    • 0036257549 scopus 로고    scopus 로고
    • Strategies for new antimicrobial proteins and peptides: lysozyme and aprotinin as model molecules
    • Ibrahim H.R., Aoki T., and Pellegrini A. Strategies for new antimicrobial proteins and peptides: lysozyme and aprotinin as model molecules. Curr. Pharm. Des. 8 (2002) 671-693
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 671-693
    • Ibrahim, H.R.1    Aoki, T.2    Pellegrini, A.3
  • 21
    • 23344433145 scopus 로고    scopus 로고
    • The polymeric immunoglobulin receptor: bridging innate and adaptive immune responses at mucosal surfaces
    • Kaetzel C.S. The polymeric immunoglobulin receptor: bridging innate and adaptive immune responses at mucosal surfaces. Immunol. Rev. 206 (2005) 83-99
    • (2005) Immunol. Rev. , vol.206 , pp. 83-99
    • Kaetzel, C.S.1
  • 22
    • 0029956059 scopus 로고    scopus 로고
    • Secretory component, the receptor for polymeric immunoglobulin, has nothing to do with beta-galactosyltransferase in human milk
    • Kobayashi K., Mafune N., Narimatsu H., Nakao H., and Taniguchi N. Secretory component, the receptor for polymeric immunoglobulin, has nothing to do with beta-galactosyltransferase in human milk. Immunol. Lett. 50 (1996) 99-104
    • (1996) Immunol. Lett. , vol.50 , pp. 99-104
    • Kobayashi, K.1    Mafune, N.2    Narimatsu, H.3    Nakao, H.4    Taniguchi, N.5
  • 23
    • 13844271888 scopus 로고    scopus 로고
    • Photocleavage of lysozyme by cobalt (III) complexes
    • Kumar C.V., and Thota J. Photocleavage of lysozyme by cobalt (III) complexes. Inorg. Chem. 44 (2005) 825-827
    • (2005) Inorg. Chem. , vol.44 , pp. 825-827
    • Kumar, C.V.1    Thota, J.2
  • 24
    • 0001281687 scopus 로고
    • Involution of the mammary gland
    • Larson B.L. (Ed), Academic Press, Inc., New York, NY
    • Lascelles A.K., and Lee C.S. Involution of the mammary gland. In: Larson B.L. (Ed). Lactation: A Comprehensive Treatise vol. IV (1978), Academic Press, Inc., New York, NY 115
    • (1978) Lactation: A Comprehensive Treatise , vol.IV , pp. 115
    • Lascelles, A.K.1    Lee, C.S.2
  • 25
    • 0031956153 scopus 로고    scopus 로고
    • Current concepts in mucosal immunity IV; How epithelial transport of IgA antibodies relates to host defense
    • Lamm M.E. Current concepts in mucosal immunity IV; How epithelial transport of IgA antibodies relates to host defense. Am. J. Physiol. 274 (1998) G614-G617
    • (1998) Am. J. Physiol. , vol.274
    • Lamm, M.E.1
  • 26
    • 0141450720 scopus 로고    scopus 로고
    • Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
    • Masschalck B., and Michiels C.W. Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria. Crit. Rev. Microbiol. 29 (2003) 191-214
    • (2003) Crit. Rev. Microbiol. , vol.29 , pp. 191-214
    • Masschalck, B.1    Michiels, C.W.2
  • 27
    • 0018590342 scopus 로고
    • Milk carbohydrates of marsupials II - qualitative and quantitative changes in milk carbohydrates during lactation in the tammar wallaby (Macropus eugenii)
    • Messer M., and Green B. Milk carbohydrates of marsupials II - qualitative and quantitative changes in milk carbohydrates during lactation in the tammar wallaby (Macropus eugenii). Aust. J. Biol. Sci. 32 (1979) 519-531
    • (1979) Aust. J. Biol. Sci. , vol.32 , pp. 519-531
    • Messer, M.1    Green, B.2
  • 28
    • 0023679490 scopus 로고
    • Studies on the carbohydrate content of milk of the crabeater seal (Lobodon carcinophagus)
    • Messer M., Crisp E.A., and Newgrain K. Studies on the carbohydrate content of milk of the crabeater seal (Lobodon carcinophagus). Comp. Biochem. Physiol. B 90 (1988) 367-370
    • (1988) Comp. Biochem. Physiol. B , vol.90 , pp. 367-370
    • Messer, M.1    Crisp, E.A.2    Newgrain, K.3
  • 30
    • 0028202474 scopus 로고
    • Transepithelial transport of immunoglobulins
    • Mostov K.E. Transepithelial transport of immunoglobulins. Annu. Rev., Immunol. 12 (1994) 63-84
    • (1994) Annu. Rev., Immunol. , vol.12 , pp. 63-84
    • Mostov, K.E.1
  • 32
    • 0002018494 scopus 로고
    • Control of milk protein synthesis in the tammar wallaby: a model to study prolactin-dependent development
    • Tyndale-Biscoe C.H., and Janssens P.A. (Eds), Springer-Verlag, Heidelberg
    • Nicholas K.R. Control of milk protein synthesis in the tammar wallaby: a model to study prolactin-dependent development. In: Tyndale-Biscoe C.H., and Janssens P.A. (Eds). The Developing Marsupial: Models for Biomedical Research (1988), Springer-Verlag, Heidelberg 68-85
    • (1988) The Developing Marsupial: Models for Biomedical Research , pp. 68-85
    • Nicholas, K.R.1
  • 33
    • 0024299520 scopus 로고
    • Asynchronous dual lactation in a Marsupial, the tammar wallaby
    • Eugenii M. (Ed)
    • Nicholas K.R. Asynchronous dual lactation in a Marsupial, the tammar wallaby. In: Eugenii M. (Ed). Biochem. Biophys. Res. Commun. 154 (1988) 529-536
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 529-536
    • Nicholas, K.R.1
  • 34
    • 0026030118 scopus 로고
    • Milk secretion in the rat: progressive changes in milk composition during lactation and weaning and the effect of diet
    • Nicholas K.R., and Hartmann P.E. Milk secretion in the rat: progressive changes in milk composition during lactation and weaning and the effect of diet. Comp. Biochem. Physiol. A 98 (1991) 535-542
    • (1991) Comp. Biochem. Physiol. A , vol.98 , pp. 535-542
    • Nicholas, K.R.1    Hartmann, P.E.2
  • 35
    • 0019880125 scopus 로고
    • Alpha-lactalbumin and lactose concentrations in rat milk during lactation
    • Nicholas K.R., Hartmann P.E., and McDonald B.L. Alpha-lactalbumin and lactose concentrations in rat milk during lactation. Biochem. J. 194 (1981) 149-154
    • (1981) Biochem. J. , vol.194 , pp. 149-154
    • Nicholas, K.R.1    Hartmann, P.E.2    McDonald, B.L.3
  • 36
    • 0024838317 scopus 로고
    • Isolation, partial sequence and asynchronous appearance during lactation of lysozyme and α-lactalbumin in the milk of a marsupial, the common ringtail possum (Pseudocheirus peregrinus)
    • Nicholas K.R., Loughnan M., Messer M., Munks S., Griffiths M., and Shaw D. Isolation, partial sequence and asynchronous appearance during lactation of lysozyme and α-lactalbumin in the milk of a marsupial, the common ringtail possum (Pseudocheirus peregrinus). Comp. Biochem. Physiol. B. 94 (1989) 775-778
    • (1989) Comp. Biochem. Physiol. B. , vol.94 , pp. 775-778
    • Nicholas, K.R.1    Loughnan, M.2    Messer, M.3    Munks, S.4    Griffiths, M.5    Shaw, D.6
  • 37
    • 0031173201 scopus 로고    scopus 로고
    • The tammar wallaby: a model to study putative autocrine-induced changes in milk composition
    • Nicholas K.R., Simpson K., Wilson M., Trott J., and Shaw D. The tammar wallaby: a model to study putative autocrine-induced changes in milk composition. J. Mammary Gland Biol. Neoplasia 2 (1997) 299-310
    • (1997) J. Mammary Gland Biol. Neoplasia , vol.2 , pp. 299-310
    • Nicholas, K.R.1    Simpson, K.2    Wilson, M.3    Trott, J.4    Shaw, D.5
  • 38
    • 0024677023 scopus 로고
    • Immunological aspects of mammary involution
    • Nickerson S.C. Immunological aspects of mammary involution. J. Dairy Sci. 72 (1989) 1665-1678
    • (1989) J. Dairy Sci. , vol.72 , pp. 1665-1678
    • Nickerson, S.C.1
  • 39
    • 0024677437 scopus 로고
    • Approaches to the manipulation of mammary involution
    • Oliver S.P., and Sordillo L.M. Approaches to the manipulation of mammary involution. J. Dairy Sci. 72 (1989) 1647-1664
    • (1989) J. Dairy Sci. , vol.72 , pp. 1647-1664
    • Oliver, S.P.1    Sordillo, L.M.2
  • 40
    • 34248527410 scopus 로고    scopus 로고
    • Stomach lysozymes of the three-toed sloth (Bradypus variegatus), an arboreal folivore from the neotropics
    • Concepcion J.L., Rangel J.D., Ruiz M.C., Michelangeli F., and Dominguez-Bello M.G. (Eds)
    • Pacheco M.A. Stomach lysozymes of the three-toed sloth (Bradypus variegatus), an arboreal folivore from the neotropics. In: Concepcion J.L., Rangel J.D., Ruiz M.C., Michelangeli F., and Dominguez-Bello M.G. (Eds). Comp. Biochem. Physiol. A 147 (2006) 808-819
    • (2006) Comp. Biochem. Physiol. A , vol.147 , pp. 808-819
    • Pacheco, M.A.1
  • 41
    • 33645670516 scopus 로고    scopus 로고
    • Human colostrum: identification of minor proteins in the aqueous phase by proteomics
    • Palmer D.J., Kelly V.C., Smit A.M., Kuy S., Knight C.G., and Cooper G.J. Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 (2006) 2208-2216
    • (2006) Proteomics , vol.6 , pp. 2208-2216
    • Palmer, D.J.1    Kelly, V.C.2    Smit, A.M.3    Kuy, S.4    Knight, C.G.5    Cooper, G.J.6
  • 42
    • 0016527796 scopus 로고
    • Recent advances in the study of monovalent ion movements across the mammary epithelium: relation to onset of lactation
    • Peaker M. Recent advances in the study of monovalent ion movements across the mammary epithelium: relation to onset of lactation. J. Dairy Sci. 58 (1975) 1042-1062
    • (1975) J. Dairy Sci. , vol.58 , pp. 1042-1062
    • Peaker, M.1
  • 43
    • 47949133360 scopus 로고
    • Lactation: some cardiovascular and metabolic consequences, and the mechanisms of lactose and ion secretion into milk
    • Breast Feeding and the Mother [Ciba Foundation Symposium 45], Elsevier, North Holland (Lloyd JK, Chairman)
    • Peaker M. Lactation: some cardiovascular and metabolic consequences, and the mechanisms of lactose and ion secretion into milk. Breast Feeding and the Mother [Ciba Foundation Symposium 45]. Excerpta Medica (1976), Elsevier, North Holland 87-101 (Lloyd JK, Chairman)
    • (1976) Excerpta Medica , pp. 87-101
    • Peaker, M.1
  • 44
    • 0005480748 scopus 로고
    • Secretions of ions and water
    • Mepham T.B. (Ed), Elsevier, Amsterdam
    • Peaker M. Secretions of ions and water. In: Mepham T.B. (Ed). Biochemistry of Lactation (1983), Elsevier, Amsterdam 285-305
    • (1983) Biochemistry of Lactation , pp. 285-305
    • Peaker, M.1
  • 45
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterisation of four bactericidal domains in the bovine β-lactoglobulin
    • Pellegrini A., Dettling C., Thomas U., and Hunziker P. Isolation and characterisation of four bactericidal domains in the bovine β-lactoglobulin. Biochem. Biophys. Acta 1526 (2001) 131-140
    • (2001) Biochem. Biophys. Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 46
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 47
    • 0015812892 scopus 로고
    • A new micromethod for determination of protein in cerebrospinal fluid and urine
    • Pesce M.A., and Strande C.S. A new micromethod for determination of protein in cerebrospinal fluid and urine. Clin. Chem. 19 (1973) 1265-1267
    • (1973) Clin. Chem. , vol.19 , pp. 1265-1267
    • Pesce, M.A.1    Strande, C.S.2
  • 48
    • 0029993248 scopus 로고    scopus 로고
    • A novel marsupial protein expressed by the mammary gland only during the early lactation and related to the kunitz proteinase inhibitors
    • Piotte C.P., and Grigor M.R. A novel marsupial protein expressed by the mammary gland only during the early lactation and related to the kunitz proteinase inhibitors. Arch. Biochem. Biophys. 330 (1996) 59-64
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 59-64
    • Piotte, C.P.1    Grigor, M.R.2
  • 49
    • 0027651495 scopus 로고
    • Diapause, pregnancy and parturition in Australian marsupials
    • Renfree M.B. Diapause, pregnancy and parturition in Australian marsupials. J. Exp. Zool. 266 (1993) 450-462
    • (1993) J. Exp. Zool. , vol.266 , pp. 450-462
    • Renfree, M.B.1
  • 50
    • 0033764066 scopus 로고    scopus 로고
    • Labelling proteins with Tc-99 m via hydrazinonicotinamide (HYNIC): optimization of the conjugation reaction
    • Rennen H.J., Boerman O.C., Koenders E.B., Oyen W.J., and Corstens F.H. Labelling proteins with Tc-99 m via hydrazinonicotinamide (HYNIC): optimization of the conjugation reaction. Nucl. Med. Biol. 27 (2000) 599-604
    • (2000) Nucl. Med. Biol. , vol.27 , pp. 599-604
    • Rennen, H.J.1    Boerman, O.C.2    Koenders, E.B.3    Oyen, W.J.4    Corstens, F.H.5
  • 51
    • 20444384801 scopus 로고    scopus 로고
    • Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo
    • Rieg S., Steffen H., Seeber S., Humeny A., Kalbacher H., Dietz K., Garbe C., and Schittek B. Deficiency of dermcidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo. J. Immunol. 174 (2005) 8003-8010
    • (2005) J. Immunol. , vol.174 , pp. 8003-8010
    • Rieg, S.1    Steffen, H.2    Seeber, S.3    Humeny, A.4    Kalbacher, H.5    Dietz, K.6    Garbe, C.7    Schittek, B.8
  • 54
    • 34248184646 scopus 로고    scopus 로고
    • Desorption electrospray ionization-mass spectrometry of proteins
    • Shin Y.S., Drolet B., Mayer R., Dolence K., and Basile F. Desorption electrospray ionization-mass spectrometry of proteins. Anal. Chem. 79 (2007) 3514-3518
    • (2007) Anal. Chem. , vol.79 , pp. 3514-3518
    • Shin, Y.S.1    Drolet, B.2    Mayer, R.3    Dolence, K.4    Basile, F.5
  • 55
    • 0034725623 scopus 로고    scopus 로고
    • The gene for a novel member of the whey acidic protein family encodes three four-disulfide core domains and is asynchronously expressed during lactation
    • Simpson K.J., Ranganathan S., Fisher J.A., Jansenns P.A., Shaw D.C., and Nicholas K.R. The gene for a novel member of the whey acidic protein family encodes three four-disulfide core domains and is asynchronously expressed during lactation. J. Biol. Chem. 275 (2000) 23074-23081
    • (2000) J. Biol. Chem. , vol.275 , pp. 23074-23081
    • Simpson, K.J.1    Ranganathan, S.2    Fisher, J.A.3    Jansenns, P.A.4    Shaw, D.C.5    Nicholas, K.R.6
  • 56
    • 0015135016 scopus 로고
    • Lactoferrin and IgG immunoglobulins from involuted bovine mammary glands
    • Smith K.L., Conrad H.R., and Porter R.M. Lactoferrin and IgG immunoglobulins from involuted bovine mammary glands. J. Dairy Sci. 54 (1971) 1427
    • (1971) J. Dairy Sci. , vol.54 , pp. 1427
    • Smith, K.L.1    Conrad, H.R.2    Porter, R.M.3
  • 57
    • 0023460953 scopus 로고
    • Secretion composition during bovine mammary involution and the relationship with mastitis
    • Sordillo L.M., Nickerson S.C., Akers R.M., and Oliver S.P. Secretion composition during bovine mammary involution and the relationship with mastitis. Int. J. Biochem. 19 (1987) 1165-1172
    • (1987) Int. J. Biochem. , vol.19 , pp. 1165-1172
    • Sordillo, L.M.1    Nickerson, S.C.2    Akers, R.M.3    Oliver, S.P.4
  • 58
    • 0028527372 scopus 로고
    • Effect of once daily milking and concurrent somatotropin on milk production and mammary tight junction permeability in cows
    • Stelwagen K., Davis S.R., Farr V.C., Eichler J., and Politis I. Effect of once daily milking and concurrent somatotropin on milk production and mammary tight junction permeability in cows. J. Dairy Sci. 77 (1994) 2995-3001
    • (1994) J. Dairy Sci. , vol.77 , pp. 2995-3001
    • Stelwagen, K.1    Davis, S.R.2    Farr, V.C.3    Eichler, J.4    Politis, I.5
  • 59
    • 0026088226 scopus 로고
    • Salivary lysozyme, lactoferrin and peroxidases: antibacterial effects on cariogenic bacteria and clinical applications in preventive dentistry
    • Tenovuo J., Lumikari M., and Soukka T. Salivary lysozyme, lactoferrin and peroxidases: antibacterial effects on cariogenic bacteria and clinical applications in preventive dentistry. Proc. Finn. Dent. Soc. 87 (1991) 197-208
    • (1991) Proc. Finn. Dent. Soc. , vol.87 , pp. 197-208
    • Tenovuo, J.1    Lumikari, M.2    Soukka, T.3
  • 60
    • 0037160516 scopus 로고    scopus 로고
    • Expression of a novel lipocalin-like milk protein gene is developmentally-regulated during lactation in the tammar wallaby (Macropus eugenii)
    • Trott J., Wilson M., Hovey R., Shaw D.C., and Nicholas K.R. Expression of a novel lipocalin-like milk protein gene is developmentally-regulated during lactation in the tammar wallaby (Macropus eugenii). Gene 283 (2002) 287-297
    • (2002) Gene , vol.283 , pp. 287-297
    • Trott, J.1    Wilson, M.2    Hovey, R.3    Shaw, D.C.4    Nicholas, K.R.5
  • 61
    • 0037369724 scopus 로고    scopus 로고
    • Maternal regulation of milk composition, milk production and pouch young development during lactation in the tammar wallaby (Macropus eugenii)
    • Trott J.F., Simpson K.J., Moyle R.L., Hearn C.M., Shaw G., Nicholas K.R., and Renfree M.B. Maternal regulation of milk composition, milk production and pouch young development during lactation in the tammar wallaby (Macropus eugenii). Biol. Reprod. 68 (2003) 929-936
    • (2003) Biol. Reprod. , vol.68 , pp. 929-936
    • Trott, J.F.1    Simpson, K.J.2    Moyle, R.L.3    Hearn, C.M.4    Shaw, G.5    Nicholas, K.R.6    Renfree, M.B.7
  • 62
    • 0025478534 scopus 로고
    • Antibacterial mechanisms of lysozyme on Streptococcus mutans
    • Wang Y.B. Antibacterial mechanisms of lysozyme on Streptococcus mutans. Zhonghua Ya Yi Xue Hui Za Zhi 9 (1990) 87-97
    • (1990) Zhonghua Ya Yi Xue Hui Za Zhi , vol.9 , pp. 87-97
    • Wang, Y.B.1
  • 63
    • 0015376963 scopus 로고
    • Concentrations of immunoglobulin in mammary secretion of ruminants during involution with particular reference to selective transfer of IgG1
    • Watson D.L., Brandon M.R., and Lascelles A.K. Concentrations of immunoglobulin in mammary secretion of ruminants during involution with particular reference to selective transfer of IgG1. Aust. J. Exp. Biol. Med. Sci. 50 (1972) 535-539
    • (1972) Aust. J. Exp. Biol. Med. Sci. , vol.50 , pp. 535-539
    • Watson, D.L.1    Brandon, M.R.2    Lascelles, A.K.3
  • 64
    • 0016918351 scopus 로고
    • Lactoferrin concentration during involution of the mammary gland
    • Welty F.K., Smith K.L., and Schanbacher F.L. Lactoferrin concentration during involution of the mammary gland. J. Dairy Sci. 59 (1976) 224-231
    • (1976) J. Dairy Sci. , vol.59 , pp. 224-231
    • Welty, F.K.1    Smith, K.L.2    Schanbacher, F.L.3
  • 65
    • 0041807041 scopus 로고
    • Changes in the quantity and composition of mammary gland secretion in the dry period between lactations
    • Wheelock J.V., Smith A., Dodd F.H., and Lyster R.L. Changes in the quantity and composition of mammary gland secretion in the dry period between lactations. J. Dairy Res. 34 (1967) 1-12
    • (1967) J. Dairy Res. , vol.34 , pp. 1-12
    • Wheelock, J.V.1    Smith, A.2    Dodd, F.H.3    Lyster, R.L.4
  • 66
    • 0023768821 scopus 로고
    • Immunohistochemical localization of IgG1, IgA and secretory component in the bovine mammary gland during involution
    • Zou S., Hurley W.L., Hegarty H.M., Larson B.L., and Nelson D.R. Immunohistochemical localization of IgG1, IgA and secretory component in the bovine mammary gland during involution. Cell Tissue Res. 251 (1988) 81-86
    • (1988) Cell Tissue Res. , vol.251 , pp. 81-86
    • Zou, S.1    Hurley, W.L.2    Hegarty, H.M.3    Larson, B.L.4    Nelson, D.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.