메뉴 건너뛰기




Volumn 17, Issue 6, 2007, Pages 617-624

Heat-induced aggregation of bovine lactoferrin at neutral pH: Effect of iron saturation

Author keywords

Iron saturation; Lactoferrin; Thermal aggregation; Thiol disulphide interchange reaction

Indexed keywords

AGGLOMERATION; DAIRY PRODUCTS; HEAT TREATMENT; IRON; PH EFFECTS; SATURATION (MATERIALS COMPOSITION); THERMODYNAMIC STABILITY;

EID: 33847030648     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2006.09.002     Document Type: Article
Times cited : (90)

References (39)
  • 2
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • Anderson B.F., Baker H.M., Norris G.E., Rice D.W., and Baker E.N. Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution. Journal of Molecular Biology 209 (1989) 711-734
    • (1989) Journal of Molecular Biology , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 3
    • 0025273624 scopus 로고
    • Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins
    • Anderson B.F., Baker H.M., Norris G.E., Rumball S.V., and Baker E.N. Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. Nature 344 (1990) 784-787
    • (1990) Nature , vol.344 , pp. 784-787
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rumball, S.V.4    Baker, E.N.5
  • 4
    • 0036188896 scopus 로고    scopus 로고
    • Lactoferrin and transferrin: Functional variations on a common structural framework
    • Baker E.N., Baker H.M., and Kidd R.D. Lactoferrin and transferrin: Functional variations on a common structural framework. Biochemistry and Cell Biology 80 (2002) 27-34
    • (2002) Biochemistry and Cell Biology , vol.80 , pp. 27-34
    • Baker, E.N.1    Baker, H.M.2    Kidd, R.D.3
  • 6
    • 0000318442 scopus 로고
    • Irreversible heat denaturation of bovine alpha-lactalbumin
    • Chaplin L.C., and Lyster R.L.J. Irreversible heat denaturation of bovine alpha-lactalbumin. Journal of Dairy Research 53 (1986) 249-258
    • (1986) Journal of Dairy Research , vol.53 , pp. 249-258
    • Chaplin, L.C.1    Lyster, R.L.J.2
  • 7
    • 0033990823 scopus 로고    scopus 로고
    • Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: A comparison with cows' and buffalo milk proteins
    • Elagamy E.I. Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: A comparison with cows' and buffalo milk proteins. Food Chemistry 68 (2000) 227-232
    • (2000) Food Chemistry , vol.68 , pp. 227-232
    • Elagamy, E.I.1
  • 8
    • 0023079986 scopus 로고
    • Cell culture assay of biological activity of lactoferrin and transferrin
    • Hashizume S., Kuroda K., and Murakami H. Cell culture assay of biological activity of lactoferrin and transferrin. Methods in Enzymology 147 (1987) 302-314
    • (1987) Methods in Enzymology , vol.147 , pp. 302-314
    • Hashizume, S.1    Kuroda, K.2    Murakami, H.3
  • 10
    • 0036230909 scopus 로고    scopus 로고
    • Changed protein structures of bovine beta-lactoglobulin B and alpha-lactalbumin as a consequence of heat treatment
    • Hong Y.H., and Creamer L.K. Changed protein structures of bovine beta-lactoglobulin B and alpha-lactalbumin as a consequence of heat treatment. International Dairy Journal 12 (2002) 345-359
    • (2002) International Dairy Journal , vol.12 , pp. 345-359
    • Hong, Y.H.1    Creamer, L.K.2
  • 13
  • 14
    • 0024232693 scopus 로고
    • Characterization of buffalo lactotransferrin by polyacrylamide-gel electrophoresis in 6-M urea
    • Kumar S., and Bhatia K.L. Characterization of buffalo lactotransferrin by polyacrylamide-gel electrophoresis in 6-M urea. Journal of Chromatography B 434 (1988) 228-231
    • (1988) Journal of Chromatography B , vol.434 , pp. 228-231
    • Kumar, S.1    Bhatia, K.L.2
  • 15
    • 0006263726 scopus 로고
    • Effects of heat treatment on structure and iron-binding capacity of bovine lactoferrin
    • International Dairy Federation, Brussels, Belgium
    • Kussendrager K.D. Effects of heat treatment on structure and iron-binding capacity of bovine lactoferrin. Indigenous antimicrobial agents of milk: Recent developments (1994), International Dairy Federation, Brussels, Belgium 133-146
    • (1994) Indigenous antimicrobial agents of milk: Recent developments , pp. 133-146
    • Kussendrager, K.D.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0003097313 scopus 로고    scopus 로고
    • On thermal stability of lactoferrin in bovine milk
    • Luf W., and Rosner E. On thermal stability of lactoferrin in bovine milk. Wiener Tierarztliche Monatsschrift 84 (1997) 70-73
    • (1997) Wiener Tierarztliche Monatsschrift , vol.84 , pp. 70-73
    • Luf, W.1    Rosner, E.2
  • 19
    • 0026699053 scopus 로고
    • High-performance liquid-chromatographic separation of human apolactoferrin and monoferric and diferric lactoferrins
    • Makino Y., and Nishimura S. High-performance liquid-chromatographic separation of human apolactoferrin and monoferric and diferric lactoferrins. Journal of Chromatography B 579 (1992) 346-349
    • (1992) Journal of Chromatography B , vol.579 , pp. 346-349
    • Makino, Y.1    Nishimura, S.2
  • 20
    • 0019153180 scopus 로고
    • Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin
    • Mazurier J., and Spik G. Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin. Biochimica et Biophysica Acta 629 (1980) 399-408
    • (1980) Biochimica et Biophysica Acta , vol.629 , pp. 399-408
    • Mazurier, J.1    Spik, G.2
  • 24
    • 0027650408 scopus 로고
    • Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes
    • Oria R., Ismail M., Sanchez L., Calvo M., and Brock J.H. Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes. Journal of Dairy Research 60 (1993) 363-369
    • (1993) Journal of Dairy Research , vol.60 , pp. 363-369
    • Oria, R.1    Ismail, M.2    Sanchez, L.3    Calvo, M.4    Brock, J.H.5
  • 25
    • 0037154651 scopus 로고    scopus 로고
    • Detection and quantitation of lactoferrin in bovine whey samples by reversed-phase high-performance liquid chromatography on polystyrene-divinylbenzene
    • Palmano K.P., and Elgar D.F. Detection and quantitation of lactoferrin in bovine whey samples by reversed-phase high-performance liquid chromatography on polystyrene-divinylbenzene. Journal of Chromatography A 947 (2002) 307-311
    • (2002) Journal of Chromatography A , vol.947 , pp. 307-311
    • Palmano, K.P.1    Elgar, D.F.2
  • 26
    • 17444399413 scopus 로고    scopus 로고
    • Effects of heat and high-hydrostatic pressure treatments on the aggregation of whey proteins in whey protein concentrate solutions
    • Patel H.A., Singh H., Anema S.G., and Creamer L.K. Effects of heat and high-hydrostatic pressure treatments on the aggregation of whey proteins in whey protein concentrate solutions. Food New Zealand 4 (2004) 29-35
    • (2004) Food New Zealand , vol.4 , pp. 29-35
    • Patel, H.A.1    Singh, H.2    Anema, S.G.3    Creamer, L.K.4
  • 27
    • 0027765190 scopus 로고
    • Thermal behaviour of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity
    • Paulson M.A., Svensson U., Kishore A.R., and Naidu A.S. Thermal behaviour of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity. Journal of Dairy Science 76 (1993) 3711-3720
    • (1993) Journal of Dairy Science , vol.76 , pp. 3711-3720
    • Paulson, M.A.1    Svensson, U.2    Kishore, A.R.3    Naidu, A.S.4
  • 28
    • 0000167389 scopus 로고
    • Heat induced interactions of milk proteins studied by differential scanning calorimetry
    • Visser H. (Ed), VCH, Weiheim, Germany
    • Paulson M., and Visser H. Heat induced interactions of milk proteins studied by differential scanning calorimetry. In: Visser H. (Ed). Protein interactions (1992), VCH, Weiheim, Germany 117-134
    • (1992) Protein interactions , pp. 117-134
    • Paulson, M.1    Visser, H.2
  • 30
    • 84976113450 scopus 로고
    • Calorimetric study of thermal-denaturation of whey proteins in simulated milk ultrafiltrate
    • Ruegg M., Moor U., and Blanc B. Calorimetric study of thermal-denaturation of whey proteins in simulated milk ultrafiltrate. Journal of Dairy Research 44 (1977) 509-520
    • (1977) Journal of Dairy Research , vol.44 , pp. 509-520
    • Ruegg, M.1    Moor, U.2    Blanc, B.3
  • 34
    • 0034492988 scopus 로고    scopus 로고
    • Occurrence, structure, biochemical properties and technological characteristics of lactoferrin
    • Steijns J.M., and van Hooijdonk A.C. Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. British Journal of Nutrition 84 Suppl. 1 (2000) S11-S17
    • (2000) British Journal of Nutrition , vol.84 , Issue.SUPPL. 1
    • Steijns, J.M.1    van Hooijdonk, A.C.2
  • 35
    • 0032431973 scopus 로고    scopus 로고
    • Reactions of denatured proteins with other cellular components to form insoluble aggregates and protection by lactoferrin
    • Takase K. Reactions of denatured proteins with other cellular components to form insoluble aggregates and protection by lactoferrin. FEBS Letters 441 (1998) 271-274
    • (1998) FEBS Letters , vol.441 , pp. 271-274
    • Takase, K.1
  • 37
    • 33847018138 scopus 로고    scopus 로고
    • Uchida, T., Sato, K., Kawasaki, Y., Dosako, S. (1996). Separation of lactoperoxidase, secretory component and lactoferrin from milk or whey with a cation exchange resin. United States Patent: 5,516,675.
  • 38
    • 0028875343 scopus 로고
    • Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis
    • van Berkel P.H., Geerts M.E., van Veen H.A., Kooiman P.M., Pieper F.R., de Boer H.A., et al. Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis. Biochemical Journal 312 (1995) 107-114
    • (1995) Biochemical Journal , vol.312 , pp. 107-114
    • van Berkel, P.H.1    Geerts, M.E.2    van Veen, H.A.3    Kooiman, P.M.4    Pieper, F.R.5    de Boer, H.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.