메뉴 건너뛰기




Volumn 71, Issue 1, 2008, Pages 126-133

Antimicrobial properties of milkfat globule membrane fractions

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS CEREUS; BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI; LACTOBACILLUS; LACTOBACILLUS ACIDOPHILUS; LACTOBACILLUS GASSERI; LISTERIA MONOCYTOGENES; LURIA; PSEUDOMONAS FLUORESCENS; SALMONELLA ENTERICA; SALMONELLA TYPHIMURIUM;

EID: 38349070921     PISSN: 0362028X     EISSN: None     Source Type: Journal    
DOI: 10.4315/0362-028X-71.1.126     Document Type: Article
Times cited : (42)

References (42)
  • 1
    • 0028220778 scopus 로고
    • Expansion of bacteriocin activity and host range of two peptides encoded within the lactacin operon
    • Allison, G. E., C. Fremaux, and T. R. Klaenhammer. 1994. Expansion of bacteriocin activity and host range of two peptides encoded within the lactacin operon. J. Bacteriol. 176:2235-2241.
    • (1994) J. Bacteriol , vol.176 , pp. 2235-2241
    • Allison, G.E.1    Fremaux, C.2    Klaenhammer, T.R.3
  • 2
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • Arnold, R. R., M. F. Cole, and J. R. McGhee. 1977. A bactericidal effect for human lactoferrin. Science 197:263-265.
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 3
    • 0020791096 scopus 로고
    • K88-mediated adhesion of E. coli inhibited by fractions in sow milk
    • Atroshi, F., R. Alaviuhkola, and M. Sandholm. 1983. K88-mediated adhesion of E. coli inhibited by fractions in sow milk. Zentbl. Vetmed. B 30:425-433.
    • (1983) Zentbl. Vetmed. B , vol.30 , pp. 425-433
    • Atroshi, F.1    Alaviuhkola, R.2    Sandholm, M.3
  • 6
    • 77956942930 scopus 로고    scopus 로고
    • Bray, R. C. 1975. Molybdenum iron-sulfur flavin hydroxylases and related enzymes, p. 299-419. In P. D. Boyer (ed.), The enzymes, 3rd ed., 12. Academic Press, San Diego, Calif.
    • Bray, R. C. 1975. Molybdenum iron-sulfur flavin hydroxylases and related enzymes, p. 299-419. In P. D. Boyer (ed.), The enzymes, 3rd ed., vol. 12. Academic Press, San Diego, Calif.
  • 7
    • 0015497562 scopus 로고
    • Iron binding proteins in milk and resistance to E. coli infections in infants
    • Bullen, J. J., H. J. Rogers, and L. Leigh. 1972. Iron binding proteins in milk and resistance to E. coli infections in infants. Br. Med. J. 1:69-75.
    • (1972) Br. Med. J , vol.1 , pp. 69-75
    • Bullen, J.J.1    Rogers, H.J.2    Leigh, L.3
  • 8
    • 0038397268 scopus 로고    scopus 로고
    • Biodefense properties of milk: The role of antimicrobial proteins and peptides
    • Clare, D. A., G. L. Catignani, and H. E. Swaisgood. 2003. Biodefense properties of milk: the role of antimicrobial proteins and peptides. Curr. Pharm. Design 9:1239-1255.
    • (2003) Curr. Pharm. Design , vol.9 , pp. 1239-1255
    • Clare, D.A.1    Catignani, G.L.2    Swaisgood, H.E.3
  • 9
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: A prospectus
    • Clare, D. A., and H. E. Swaisgood. 2000. Bioactive milk peptides: a prospectus. J Dairy Sci. 83:1187-1195.
    • (2000) J Dairy Sci , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 11
    • 0141918811 scopus 로고    scopus 로고
    • Lactoferrin - a multifunctional protein with antimicrobial properties
    • Farnaud, S., and R. W. Evans. 2003. Lactoferrin - a multifunctional protein with antimicrobial properties. Mol. Immunol. 40:395-405.
    • (2003) Mol. Immunol , vol.40 , pp. 395-405
    • Farnaud, S.1    Evans, R.W.2
  • 12
    • 0042525754 scopus 로고    scopus 로고
    • The screening of hydrogen peroxide-producing lactic acid bacteria and their application to inactivating psychrotrophic food-borne pathogens
    • Ito, A., Y. Sato, S. Kudo, S. Sato, H. Nakajima, and T. Toba. 2003. The screening of hydrogen peroxide-producing lactic acid bacteria and their application to inactivating psychrotrophic food-borne pathogens. Curr. Microbiol. 47:231-246.
    • (2003) Curr. Microbiol , vol.47 , pp. 231-246
    • Ito, A.1    Sato, Y.2    Kudo, S.3    Sato, S.4    Nakajima, H.5    Toba, T.6
  • 13
    • 84988123086 scopus 로고
    • Analysis and optimization of methods using water-soluble carbodiimide for immobilization of biochemicals to porous glass
    • Janolino, V. G., and H. E. Swaisgood. 1982. Analysis and optimization of methods using water-soluble carbodiimide for immobilization of biochemicals to porous glass. Biotechnol. Bioeng. 24:1069-1080.
    • (1982) Biotechnol. Bioeng , vol.24 , pp. 1069-1080
    • Janolino, V.G.1    Swaisgood, H.E.2
  • 14
    • 85036981347 scopus 로고    scopus 로고
    • Keenan, T. W., and S. Patton. 1995. The structure of milk: implications for sampling and storage. The milk lipid globule, p. 5-50. In R. G. Jensen, (ed.), Handbook of milk composition. Academic Press, New York.
    • Keenan, T. W., and S. Patton. 1995. The structure of milk: implications for sampling and storage. The milk lipid globule, p. 5-50. In R. G. Jensen, (ed.), Handbook of milk composition. Academic Press, New York.
  • 15
    • 84976163912 scopus 로고
    • Fractionation and characterization of the membranes for bovine milk fat globules
    • Kitchen, B. J. 1977. Fractionation and characterization of the membranes for bovine milk fat globules. J. Dairy Res. 44:469-482.
    • (1977) J. Dairy Res , vol.44 , pp. 469-482
    • Kitchen, B.J.1
  • 16
    • 0034492989 scopus 로고    scopus 로고
    • Lactoperoxidase: Physio-chemical properties, occurrence, mechanism of action and applications
    • Kussendrager, K. D., and A. C. M. van Hooijdonk. 2000. Lactoperoxidase: physio-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 84(Suppl. 1):S1-S25.
    • (2000) Br. J. Nutr , vol.84 , Issue.SUPPL. 1
    • Kussendrager, K.D.1    van Hooijdonk, A.C.M.2
  • 17
    • 0000114733 scopus 로고
    • The antibacterial effect of enzymatic xanthine oxidase
    • Lipmann, F., and C. R. Owen. 1943. The antibacterial effect of enzymatic xanthine oxidase. Science 98:246-248.
    • (1943) Science , vol.98 , pp. 246-248
    • Lipmann, F.1    Owen, C.R.2
  • 18
    • 0022371729 scopus 로고
    • Biochemical and physiological function of human milk proteins
    • Lonnerdal, B. 1985. Biochemical and physiological function of human milk proteins. Am. J. Clin. Nutr. 42:1299-1317.
    • (1985) Am. J. Clin. Nutr , vol.42 , pp. 1299-1317
    • Lonnerdal, B.1
  • 19
    • 0019297273 scopus 로고
    • Comparison of the antibacterial activity of the hypothiocyanate anion towards Streptococcus lactis and Escherichia coli
    • Marshall, V. M. E., and B. Reiter. 1980. Comparison of the antibacterial activity of the hypothiocyanate anion towards Streptococcus lactis and Escherichia coli. J. Gen. Microbiol. 120:513-516.
    • (1980) J. Gen. Microbiol , vol.120 , pp. 513-516
    • Marshall, V.M.E.1    Reiter, B.2
  • 20
    • 0016712345 scopus 로고
    • Studies on the structure of milk fat globule membrane
    • Mather, I. H., and T. W. Keenan. 1975. Studies on the structure of milk fat globule membrane. J. Membrane Biol. 21:65-85.
    • (1975) J. Membrane Biol , vol.21 , pp. 65-85
    • Mather, I.H.1    Keenan, T.W.2
  • 21
    • 0017470607 scopus 로고
    • Membranes of mammary gland. XII. Loosely associated proteins and compositional heterogeneity of bovine milk fat globule membrane
    • Mather, I. H., K. Weber, and T. W. Keenan. 1977. Membranes of mammary gland. XII. Loosely associated proteins and compositional heterogeneity of bovine milk fat globule membrane. J. Dairy Sci. 60:394-402.
    • (1977) J. Dairy Sci , vol.60 , pp. 394-402
    • Mather, I.H.1    Weber, K.2    Keenan, T.W.3
  • 22
    • 77956856274 scopus 로고
    • Methods for studying bacteriocins
    • J. R. Morris and D. W. Ribbons ed, Academic Press, New York
    • Mayr-Harting, A., A. J. Hedges, and R. C. W. Berkeley. 1972. Methods for studying bacteriocins, p. 315-422. In J. R. Morris and D. W. Ribbons (ed.), Methods in Microbiology, vol. 7A. Academic Press, New York.
    • (1972) Methods in Microbiology , vol.7 A , pp. 315-422
    • Mayr-Harting, A.1    Hedges, A.J.2    Berkeley, R.C.W.3
  • 23
    • 0014410114 scopus 로고
    • The reduction of cytochrome c by milk xanthine oxidase
    • McCord, J. M., and I. Fridovich. 1968. The reduction of cytochrome c by milk xanthine oxidase. J. Biol. Chem. 243:5753-5760.
    • (1968) J. Biol. Chem , vol.243 , pp. 5753-5760
    • McCord, J.M.1    Fridovich, I.2
  • 24
    • 0025811817 scopus 로고
    • Lysozyme and alpha-lactalbumin: Structure, function, and interrelationships
    • McKenzie, H. A., and F. H. White, Jr. 1991. Lysozyme and alpha-lactalbumin: structure, function, and interrelationships. Adv. Protein Chem. 41:173-315.
    • (1991) Adv. Protein Chem , vol.41 , pp. 173-315
    • McKenzie, H.A.1    White Jr., F.H.2
  • 25
    • 0030749136 scopus 로고    scopus 로고
    • Biochemical properties of regulatory peptides derived from milk proteins
    • Meisel, H. 1997. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 43:119-128.
    • (1997) Biopolymers , vol.43 , pp. 119-128
    • Meisel, H.1
  • 26
    • 0017749210 scopus 로고
    • Glucose transport in Streptococcus agalactiae and its inhibition by lactoperoxidase-thiocyanate-hydrogen peroxide
    • Mickelson, M. N. 1977. Glucose transport in Streptococcus agalactiae and its inhibition by lactoperoxidase-thiocyanate-hydrogen peroxide. J. Bacteriol. 132:541-548.
    • (1977) J. Bacteriol , vol.132 , pp. 541-548
    • Mickelson, M.N.1
  • 27
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin
    • Pellegrini, A., C. Dettling, U. Thomas, and P. Hunziker. 2001. Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochim. Biophys. Acta 1526:131-140.
    • (2001) Biochim. Biophys. Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 28
    • 0023688014 scopus 로고
    • Ancient origin of lactalbumin from lysozyme: Analysis of DNA and amino acid sequences
    • Prager, E. M., and A. C. Wilson. 1988. Ancient origin of lactalbumin from lysozyme: analysis of DNA and amino acid sequences. J. Mol. Evol. 27:326-335.
    • (1988) J. Mol. Evol , vol.27 , pp. 326-335
    • Prager, E.M.1    Wilson, A.C.2
  • 29
    • 0003059628 scopus 로고
    • Inhibition of Pseudomonas species by hydrogen peroxide producing IactobaciIIi
    • Price, R. J., and J. S. Lee. 1970. Inhibition of Pseudomonas species by hydrogen peroxide producing IactobaciIIi. J. Milk Food Technol. 33:13-18.
    • (1970) J. Milk Food Technol , vol.33 , pp. 13-18
    • Price, R.J.1    Lee, J.S.2
  • 30
    • 0018065656 scopus 로고
    • Review of nonspecific antimicrobial factors in colostrum
    • Reiter, B. 1978. Review of nonspecific antimicrobial factors in colostrum. Ann. Rech. Vet. 9:205-224.
    • (1978) Ann. Rech. Vet , vol.9 , pp. 205-224
    • Reiter, B.1
  • 31
    • 0017239932 scopus 로고
    • Non-specific bactericidal activity of the lactoperoxidase-thiocyanate-hydrogen peroxide system of milk against Escherichia coli and some gram-negative pathogens
    • Reiter, B., V. M. Marshall, L. Bjorck, and C. G. Rosen. 1976. Non-specific bactericidal activity of the lactoperoxidase-thiocyanate-hydrogen peroxide system of milk against Escherichia coli and some gram-negative pathogens. Infect. Immun. 13:800-807.
    • (1976) Infect. Immun , vol.13 , pp. 800-807
    • Reiter, B.1    Marshall, V.M.2    Bjorck, L.3    Rosen, C.G.4
  • 33
    • 0026695688 scopus 로고
    • Inhibition of adhesion of S-fimbriated Escherichia coli to buccal epithelial cells by human milk fat globule membrane components: A novel aspect of protective functions in the nonimmunoglobulin fraction
    • Schroten, H., F. G. Hanisch, R. Plogmann, G. Uhlenbruck, R. Nobis-Bosch, and V. Wahn. 1992. Inhibition of adhesion of S-fimbriated Escherichia coli to buccal epithelial cells by human milk fat globule membrane components: a novel aspect of protective functions in the nonimmunoglobulin fraction. Infect. Immun. 60:2893-2899.
    • (1992) Infect. Immun , vol.60 , pp. 2893-2899
    • Schroten, H.1    Hanisch, F.G.2    Plogmann, R.3    Uhlenbruck, G.4    Nobis-Bosch, R.5    Wahn, V.6
  • 35
    • 1642388498 scopus 로고    scopus 로고
    • Metabolic and biochemical responses of probiotic bacteria to oxygen
    • Talwalkar, A., and K. Kailasapathy. 2003. Metabolic and biochemical responses of probiotic bacteria to oxygen. J. Dairy Sci. 86:2537-2546.
    • (2003) J. Dairy Sci , vol.86 , pp. 2537-2546
    • Talwalkar, A.1    Kailasapathy, K.2
  • 36
    • 0035964991 scopus 로고    scopus 로고
    • Inhibitory activity of honey against foodborne pathogens influenced by the presence of hydrogen peroxide and level of antioxidant power
    • Taormina, P. J., B. A. Niemira, and L. R. Beuchat. 2001. Inhibitory activity of honey against foodborne pathogens influenced by the presence of hydrogen peroxide and level of antioxidant power. Int. J. Food Microbiol. 69:217-225.
    • (2001) Int. J. Food Microbiol , vol.69 , pp. 217-225
    • Taormina, P.J.1    Niemira, B.A.2    Beuchat, L.R.3
  • 37
    • 0019478864 scopus 로고
    • Peroxidase antimicrobial system of human saliva: Requirements for accumulation of hypothiocyanite
    • Thomas, E. L., K. P. Bates, and N. M. Jefferson. 1981. Peroxidase antimicrobial system of human saliva: requirements for accumulation of hypothiocyanite. J. Dental Res. 60:785-796.
    • (1981) J. Dental Res , vol.60 , pp. 785-796
    • Thomas, E.L.1    Bates, K.P.2    Jefferson, N.M.3
  • 38
    • 0024570531 scopus 로고
    • Digestibilities of the protein in various foods as determined in vitro by an immobilized digestive enzyme assay (IDEA)
    • Thresher, W. C., H. E. Swaisgood, and G. L. Catignani. 1989. Digestibilities of the protein in various foods as determined in vitro by an immobilized digestive enzyme assay (IDEA). Plant Foods Hum. Nutr. 39:59-65.
    • (1989) Plant Foods Hum. Nutr , vol.39 , pp. 59-65
    • Thresher, W.C.1    Swaisgood, H.E.2    Catignani, G.L.3
  • 39
    • 0035036797 scopus 로고    scopus 로고
    • Inhibition of Helicobacter pylori infection by bovine milk glycoconjugates in a Balb/cA mouse model
    • Wang, X., S. Hirmo, R. Willen, and T. Wadstrom. 2001. Inhibition of Helicobacter pylori infection by bovine milk glycoconjugates in a Balb/cA mouse model. J. Med. Microbiol. 50:430-435.
    • (2001) J. Med. Microbiol , vol.50 , pp. 430-435
    • Wang, X.1    Hirmo, S.2    Willen, R.3    Wadstrom, T.4
  • 40
    • 0014542981 scopus 로고
    • Action of hydrogen peroxide on growth inhibition of Salmonella typhimurium
    • Watson, J. A., and J. Schubert. 1969. Action of hydrogen peroxide on growth inhibition of Salmonella typhimurium. J. Gen. Microbiol. 57:25-34.
    • (1969) J. Gen. Microbiol , vol.57 , pp. 25-34
    • Watson, J.A.1    Schubert, J.2
  • 41
    • 0016743512 scopus 로고
    • A new purification procedure for bovine milk xanthine oxidase: Effect of proteolysis on the subunit structure
    • Waud, W. R., F. O. Brady, R. D. Wiley, and K. V. Rajagopalan. 1975. A new purification procedure for bovine milk xanthine oxidase: effect of proteolysis on the subunit structure. Arch. Biochem. Biophys. 169:695-701.
    • (1975) Arch. Biochem. Biophys , vol.169 , pp. 695-701
    • Waud, W.R.1    Brady, F.O.2    Wiley, R.D.3    Rajagopalan, K.V.4
  • 42
    • 38349018187 scopus 로고
    • Enzyme manual
    • Worthington Biochemical Corp, Worthington Biochemical Corp, Freehold, N.J
    • Worthington Biochemical Corp. 1972. Enzyme manual. Enzymes, enzyme reagents, and related biochemicals. Worthington Biochemical Corp., Freehold, N.J.
    • (1972) Enzymes, enzyme reagents, and related biochemicals


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.