메뉴 건너뛰기




Volumn 141, Issue 3, 2013, Pages 3007-3013

Physico-chemical properties of different forms of bovine lactoferrin

Author keywords

Lactoferrin; Molecular confirmation; Physico chemical properties; Rheological behaviour; Surface tension; Thermal denaturation

Indexed keywords

DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; IRON; MAMMALS; PH; SOLUTIONS; SURFACE TENSION;

EID: 84879486580     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.05.139     Document Type: Article
Times cited : (106)

References (33)
  • 2
    • 28344440468 scopus 로고    scopus 로고
    • Molecular structure, binding properties and dynamics of lactoferrin
    • DOI 10.1007/s00018-005-5368-9
    • Baker, E. N., & Baker, H. M. (2005). Molecular structure, binding properties and dynamics of Lactoferrin. Cellular and Molecular Life Sciences, 62, 2531-2539. (Pubitemid 41721228)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2531-2539
    • Baker, E.N.1    Baker, H.M.2
  • 3
    • 0015919687 scopus 로고
    • The reaction of ferric salts with transferrin
    • Bates, G. W., & Schlabach, M. R. (1973). The reaction of ferric salts with transferrin. Journal of Biological Chemistry, 248(9), 3228-3232.
    • (1973) Journal of Biological Chemistry , vol.248 , Issue.9 , pp. 3228-3232
    • Bates, G.W.1    Schlabach, M.R.2
  • 4
    • 79952535799 scopus 로고    scopus 로고
    • Formation of protein nanoparticles by control led heat treatment of lactoferrin: Factors affecting particle characteristics
    • Bengoechea, C., Peinado, I., & McClements, D. J. (2011). Formation of protein nanoparticles by control led heat treatment of lactoferrin: Factors affecting particle characteristics. Food Hydrocolloids, 25(5), 1354-1360.
    • (2011) Food Hydrocolloids , vol.25 , Issue.5 , pp. 1354-1360
    • Bengoechea, C.1    Peinado, I.2    McClements, D.J.3
  • 5
    • 0024347869 scopus 로고
    • Lactoferrin from human breast milk and from neutrophil granulocytes. Comparative studies of isolation, quantitation, characterization and iron binding properties
    • Bezwoda, W. R., & Mansoor, N. (1989). Lactoferrin from human breast milk and from neutrophil granulocy tes. Comparative studies of isolation, quantitation, characterization and iron binding properties. Biomedical Chromatography, 3(3), 121-126. (Pubitemid 19196278)
    • (1989) Biomedical Chromatography , vol.3 , Issue.3 , pp. 121-126
    • Bezwoda, W.R.1    Mansoor, N.2
  • 6
    • 84884594907 scopus 로고    scopus 로고
    • Quantification and elucidation of the overall interaction between nanoparticles
    • V. M. Starov (Ed.) Boca Raton, Florida: CRC Press
    • Bowen, W. R., & Williams, P. M. (2010). Quantification and elucidation of the overall interaction between nanoparticles. In V. M. Starov (Ed.), Nanoscience: Colloidal and Interfacial Aspects (pp. 79-98). Boca Raton, Florida: CRC Press.
    • (2010) Nanoscience: Colloidal and Interfacial Aspects , pp. 79-98
    • Bowen, W.R.1    Williams, P.M.2
  • 7
    • 33847030648 scopus 로고    scopus 로고
    • Heat-induced aggregation of bovine lactoferrin at neutral pH: Effect of iron saturation
    • DOI 10.1016/j.idairyj.2006.09.002, PII S0958694606002123
    • Brisson, G., Britten, M., & Pouliot, Y. (2007). Heat- induced aggregation of bovine lactoferrin at neutral pH: Effect of iron saturation. International Dairy Journal, 17(6), 617-624. (Pubitemid 46274287)
    • (2007) International Dairy Journal , vol.17 , Issue.6 , pp. 617-624
    • Brisson, G.1    Britten, M.2    Pouliot, Y.3
  • 8
    • 0036191387 scopus 로고    scopus 로고
    • The physiology of lactoferrin
    • DOI 10.1139/o01-212
    • Brock, J. H. (2002). The physiology of lactoferrin. Biochemistry and Cell Biology, 80, 1-6. (Pubitemid 34194221)
    • (2002) Biochemistry and Cell Biology , vol.80 , Issue.1 , pp. 1-6
    • Brock, J.H.1
  • 9
    • 0016174518 scopus 로고
    • Spectroscopic study of bovine lactoferrin
    • Brown, E. M., & Parry, R. M. (1974). Spectroscopic study of bovine lactoferrin. Biochemistry, 13(22), 4560-4565.
    • (1974) Biochemistry , vol.13 , Issue.22 , pp. 4560-4565
    • Brown, E.M.1    Parry, R.M.2
  • 11
    • 27844568472 scopus 로고    scopus 로고
    • Human tear viscosity: An interactive role for proteins and lipids
    • DOI 10.1016/j.bbapap.2005.08.023, PII S1570963905003262
    • Gouveia, S. M., & Tiffany, J. M. (2005). Human tear viscosity: An interactive role for proteins and lipids. Biochimica et Biophysica Acta, 1753, 155-163. (Pubitemid 41643149)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1753 , Issue.2 , pp. 155-163
    • Gouveia, S.M.1    Tiffany, J.M.2
  • 12
    • 0001395327 scopus 로고
    • The isolation of a red protein from milk
    • Groves, M. L. (1960). The isolation of a red protein from milk. Journal of the American Chemical Society, 82(13), 3345-3350.
    • (1960) Journal of the American Chemical Society , vol.82 , Issue.13 , pp. 3345-3350
    • Groves, M.L.1
  • 13
    • 0023079986 scopus 로고
    • Cell culture ass ay of biological activity of lactoferrin and transferrin
    • Hashizume, S., Kuroda, K., & Murakami, H. (1987). Cell culture ass ay of biological activity of lactoferrin and transferrin. Methods in Enzymology, 147, 302-314.
    • (1987) Methods in Enzymology , vol.147 , pp. 302-314
    • Hashizume, S.1    Kuroda, K.2    Murakami, H.3
  • 14
    • 48849088860 scopus 로고    scopus 로고
    • Studies of the structure of multiferric ion-bound lactoferrin: A new antianemic edible material
    • Hu, F., Pan, F., Sawano, Y., Makino, T., Kakehi, Y., Komiyama, M., et al. (2008). Studies of the structure of multiferric ion-bound lactoferrin: A new antianemic edible material. International Dairy Journal, 18, 1051-10 56.
    • (2008) International Dairy Journal , vol.18 , pp. 1051-1056
    • Hu, F.1    Pan, F.2    Sawano, Y.3    Makino, T.4    Kakehi, Y.5    Komiyama, M.6
  • 16
    • 0001186821 scopus 로고
    • Functional properties of proteins: Possible relationships between structure and function in foams
    • Kinsella, J. E. (1981). Functional properties of proteins: Possible relationships between structure and function in foams. Food Chemistry, 7, 273-288.
    • (1981) Food Chemistry , vol.7 , pp. 273-288
    • Kinsella, J.E.1
  • 17
    • 0000468776 scopus 로고
    • Reporting of objective colour measurements
    • McGuire, R. G. (1992). Reporting of objective colour measurements. Horticultural Science, 27(12), 1254-1255.
    • (1992) Horticultural Science , vol.27 , Issue.12 , pp. 1254-1255
    • McGuire, R.G.1
  • 19
    • 0030719461 scopus 로고    scopus 로고
    • Three-dimensional structure of diferric bovine lactoferrin at 2.8 resolution
    • DOI 10.1006/jmbi.1997.1386
    • Moore, S. A., Anderson, B. F., Groom, C. R., Haridas, M., & Baker, E. N. (1997). Threedimensional structure of diferric bovine lactoferr in at 2.8 Å resolution. Journal of Molecular Biology, 274(2), 222-236. (Pubitemid 27520608)
    • (1997) Journal of Molecular Biology , vol.274 , Issue.2 , pp. 222-236
    • Moore, S.A.1    Anderson, B.F.2    Groom, C.R.3    Haridas, M.4    Baker, E.N.5
  • 21
    • 77956092764 scopus 로고    scopus 로고
    • Fabrication and morphological characterization of biopolymer particles formed by electrostatic complexation of heat treated lactoferrin and anionic polysaccharides
    • Peinado, I., Lesmes, U., Andrés, A., & McClements, J. D. (2010). Fabrication and morphological characterization of biopolymer particles formed by electrostatic complexation of heat treated lactoferrin and anionic polysaccharides. Langmuir, 26(12), 9827-9834.
    • (2010) Langmuir , vol.26 , Issue.12 , pp. 9827-9834
    • Peinado, I.1    Lesmes, U.2    Andrés, A.3    McClements, J.D.4
  • 23
    • 84976113450 scopus 로고
    • A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate
    • Rüegg, M., Moor, U., & Blanc, B. (1977). A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate. Journal of Dairy Research, 44(03), 509-520.
    • (1977) Journal of Dairy Research , vol.44 , Issue.3 , pp. 509-520
    • Rüegg, M.1    Moor, U.2    Blanc, B.3
  • 25
    • 0026099978 scopus 로고
    • Comparison of bovine, sheep and goat milk lactoferrins in their electrophoretic behavior, conformation, immunochemical properties and lectin reactivity
    • Shimazaki, K.-I., Kawano, N., & Yoo, Y. C. (1991). Comparison of bovine, sheep and goat milk lactoferrins in their electrophoretic behavior, conformation, immunochemical properties and lectin reactivity. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 98(2-3), 417-422.
    • (1991) Comparative Biochemistry and Physiology Part B: Comparative Biochemistry , vol.98 , Issue.2-3 , pp. 417-422
    • Shimazaki, K.-I.1    Kawano, N.2    Yoo, Y.C.3
  • 26
    • 0027585645 scopus 로고
    • Separation and characterisation of the C-terminal half molecule of bovine lactoferrin
    • Shimazaki K.-I ., Tanaka, T., Kon, H., Oota, K., Kawaguchi, A., Maki, Y., et al. (1993). Separation and characterisation of the C-terminal half molecule of bovine lactoferrin. Journal of Dairy Science, 76(4), 946-95 5.
    • (1993) Journal of Dairy Science , vol.76 , Issue.4 , pp. 946-955
    • Shimazaki, K.-I.1    Tanaka, T.2    Kon, H.3    Oota, K.4    Kawaguchi, A.5    Maki, Y.6
  • 27
    • 0034492988 scopus 로고    scopus 로고
    • Occurrence, structure, biochemical properties and technological characteristics of lactoferrin
    • Steijns, J. M., & van Hooijdonk, A. C. M. (2000). Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. British Journal of Nutrition, 84(Supplement S1), 11-17.
    • (2000) British Journal of Nutrition , vol.84 , Issue.SUPPL. S1 , pp. 11-17
    • Steijns, J.M.1    Van Hooijdonk, A.C.M.2
  • 28
    • 79952532377 scopus 로고    scopus 로고
    • Physicochemical properties of lactoferrin stabilized oil-in-water emulsions: Effects of pH, salt and heating
    • Tokle, T., & McClements, D. J. (2011). Physicochemical properties of lactoferrin stabilized oil-in-water emulsions: Effects of pH, salt and heating. Food Hydrocolloids, 25(5), 976-982.
    • (2011) Food Hydrocolloids , vol.25 , Issue.5 , pp. 976-982
    • Tokle, T.1    McClements, D.J.2
  • 29
    • 0002123958 scopus 로고
    • Adsorption of globular proteins at the air/water interface as measured via dynamic surface tension: Concentration dependence, mass-transfer considerations, and adsorption kinetics
    • Tripp, B. C., Magda J. J., & Andrade, J. D. (1995). Adsorption of globular proteins at the air/water interface as measured via dynamic surface tension: concentration dependence, mass-transfer considerations, and adsorption kinetics. Journal of colloid and inte rface science, 173, 16-27.
    • (1995) Journal of Colloid and Interface Science , vol.173 , pp. 16-27
    • Tripp, B.C.1    Magda, J.J.2    Andrade, J.D.3
  • 30
    • 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. C., Geerts, M. E. J., van Veen, H. A., Kooiman, P. M., Pieper, F. R., De Boer, H. A., et al. (1995). 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, 107-114.
    • (1995) Biochemical Journal , vol.312 , pp. 107-114
    • Van Berkel, P.H.C.1    Geerts, M.E.J.2    Van Veen, H.A.3    Kooiman, P.M.4    Pieper, F.R.5    De Boer, H.A.6
  • 31
    • 33748325910 scopus 로고    scopus 로고
    • Lactoferrin research, technology and applications
    • DOI 10.1016/j.idairyj.2006.06.013, PII S0958694606001579
    • Wakabayashi, H., Yamauchi, K., & Takase, M. (2006). Lactoferrin research, technology and applications. International Dairy Journal, 16, 1241-1251. (Pubitemid 44331588)
    • (2006) International Dairy Journal , vol.16 , Issue.11 , pp. 1241-1251
    • Wakabayashi, H.1    Yamauchi, K.2    Takase, M.3
  • 32
    • 0026785065 scopus 로고
    • Skin colour measurements in terms of CIELAB colour space values
    • Weatherall, I. L., & Coombs, B. D. (1992). Skin colour measurements in terms of CIELAB colour space values. Journal of Investigative Dermatology, 99(4), 468-473.
    • (1992) Journal of Investigative Dermatology , vol.99 , Issue.4 , pp. 468-473
    • Weatherall, I.L.1    Coombs, B.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.