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Volumn 152, Issue , 2014, Pages 121-127

Evaluation of different methods for determination of the iron saturation level in bovine lactoferrin

Author keywords

Colour space parameters; Ellipticity; Enthalpy of denaturation; Iron saturation; Lactoferrin; Polar coordinates

Indexed keywords

COLOR; DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; MAMMALS; REGRESSION ANALYSIS;

EID: 84890499538     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.11.132     Document Type: Article
Times cited : (25)

References (31)
  • 2
    • 0019218291 scopus 로고
    • Studies on human lactoferrin by electron paramagnetic resonance, fluorescence, and resonance raman spectroscopy
    • DOI 10.1021/bi00558a026
    • E.W. Ainscough, A.M. Brodie, J.E. Plowman, S.J. Bloor, J.S. Loehr, and T.M. Loehr Studies on human lactoferrin by electron paramagnetic resonance, fluorescence, and resonance Raman spectroscopy Biochemistry 19 17 1980 4072 4079 (Pubitemid 11242467)
    • (1980) Biochemistry , vol.19 , Issue.17 , pp. 4072-4079
    • Ainscough, E.W.1    Brodie, A.M.2    Plowman, J.E.3
  • 3
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • DOI 10.1016/0022-2836(89)90602-5
    • B.F. Anderson, H.M. Baker, G.E. Norris, D.W. Rice, and E.N. Baker Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution Journal of Molecular Biology 209 4 1989 711 734 (Pubitemid 20046127)
    • (1989) Journal of Molecular Biology , vol.209 , Issue.4 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 4
    • 28344440468 scopus 로고    scopus 로고
    • Molecular structure, binding properties and dynamics of lactoferrin
    • DOI 10.1007/s00018-005-5368-9
    • E.N. Baker, and H.M. Baker Molecular structure, binding properties and dynamics of Lactoferrin Cellular and Molecular Life Sciences 62 2005 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
  • 5
    • 79952535799 scopus 로고    scopus 로고
    • Formation of protein nanoparticles by controlled heat treatment of lactoferrin: Factors affecting particle characteristics
    • C. Bengoechea, I. Peinado, and D.J. McClements Formation of protein nanoparticles by controlled heat treatment of lactoferrin: Factors affecting particle characteristics Food Hydrocolloids 25 5 2011 1354 1360
    • (2011) Food Hydrocolloids , vol.25 , Issue.5 , pp. 1354-1360
    • Bengoechea, C.1    Peinado, I.2    McClements, D.J.3
  • 6
    • 84879486580 scopus 로고    scopus 로고
    • Physico-chemical properties of different forms of bovine lactoferrin
    • H. Bokkhim, N. Bansal, L. Grøndahl, and B. Bhandari Physico-chemical properties of different forms of bovine lactoferrin Food Chemistry 141 2013 3007 3013
    • (2013) Food Chemistry , vol.141 , pp. 3007-3013
    • Bokkhim, H.1    Bansal, N.2    Groslash3    ndahl, L.4    Bhandari, B.5
  • 7
    • 0034045917 scopus 로고    scopus 로고
    • Iron absorption from ferrous bisglycinate and ferric trisglycinate in whole maize is regulated by iron status
    • A.C. Bovell-Benjamin, F.E. Viteri, and L.H. Allen Iron absorption from ferrous bisglycinate and ferric trisglycinate in whole maize is regulated by iron status American Journal of Clinical Nutrition 71 2000 1563 1569 (Pubitemid 30395905)
    • (2000) American Journal of Clinical Nutrition , vol.71 , Issue.6 , pp. 1563-1569
    • Bovell-Benjamin, A.C.1    Viteri, F.E.2    Allen, L.H.3
  • 8
    • 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
    • G. Brisson, M. Britten, and Y. Pouliot Heat-induced aggregation of bovine lactoferrin at neutral pH: Effect of iron saturation International Dairy Journal 17 6 2007 617 624 (Pubitemid 46274287)
    • (2007) International Dairy Journal , vol.17 , Issue.6 , pp. 617-624
    • Brisson, G.1    Britten, M.2    Pouliot, Y.3
  • 9
    • 0016174518 scopus 로고
    • Spectroscopic study of bovine lactoferrin
    • E.M. Brown, and R.M. Parry Spectroscopic study of bovine lactoferrin Biochemistry 13 22 1974 4560 4565
    • (1974) Biochemistry , vol.13 , Issue.22 , pp. 4560-4565
    • Brown, E.M.1    Parry, R.M.2
  • 11
    • 0028293048 scopus 로고
    • Fourier transform infrared spectroscopy and differential scanning calorimetry of transferrins: Human serum transferrin, rabbit serum transferrin and human lactoferrin
    • DOI 10.1016/0167-4838(94)90092-2
    • J.M. Hadden, M. Bloemendal, P.I. Haris, S.K.S. Srai, and D. Chapman Fourier transform infrared spectroscopy and differential scanning calorimetry of transferrins: Human serum transferrin, rabbit serum transferrin and human lactoferrin Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1205 1 1994 59 67 (Pubitemid 24090684)
    • (1994) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1205 , Issue.1 , pp. 59-67
    • Hadden, J.M.1    Bloemendal, M.2    Haris, P.I.3    Srai, S.K.S.4    Chapman, D.5
  • 12
    • 0023079986 scopus 로고
    • Cell culture assay of biological activity of lactoferrin and transferrin
    • S. Hashizume, K. Kuroda, and H. Murakami Cell culture assay of biological activity of lactoferrin and transferrin Methods in Ezymology 147 1987 302 314
    • (1987) Methods in Ezymology , vol.147 , pp. 302-314
    • Hashizume, S.1    Kuroda, K.2    Murakami, H.3
  • 13
    • 33748463955 scopus 로고    scopus 로고
    • Optical biosensor analysis of the heat denaturation of bovine lactoferrin
    • DOI 10.1016/j.foodchem.2005.12.025, PII S030881460600015X
    • H.E. Indyk, I.J. McGrail, G.A. Watene, and E.L. Filonzi Optical biosensor analysis of the heat denaturation of bovine lactoferrin Food Chemistry 101 2 2007 838 844 (Pubitemid 44349108)
    • (2007) Food Chemistry , vol.101 , Issue.2 , pp. 838-844
    • Indyk, H.E.1    McGrail, I.J.2    Watene, G.A.3    Filonzi, E.L.4
  • 14
    • 0024232693 scopus 로고
    • Characterization of buffalo lactotransferrin by polyacrylamide gel electrophoresis in 6 M urea
    • DOI 10.1016/0378-4347(88)80080-X
    • S. Kumar, and K.L. Bhatia Characterization of buffalo lactotransferrin by polyacrylaminde gel electrophoresis in 6 M urea Journal of Chromatography 434 1988 228 231 (Pubitemid 19036879)
    • (1988) Journal of Chromatography - Biomedical Applications , vol.434 , Issue.1 , pp. 228-231
    • Kumar, S.1    Bhatia, K.L.2
  • 16
    • 0026699053 scopus 로고
    • High-performance liquid chromatographic separation of human apolactoferrin and monoferric and diferric lactoferrins
    • Y. Makino, and S. Nishimura High-performance liquid chromatographic separation of human apolactoferrin and monoferric and diferric lactoferrins Journal of Chromatography 579 1992 346 349
    • (1992) Journal of Chromatography , vol.579 , pp. 346-349
    • Makino, Y.1    Nishimura, S.2
  • 17
    • 0019153180 scopus 로고
    • Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin
    • J. Mazurier, and G. Spik 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 (BBA) - General Subjects 629 2 1980 399 408 (Pubitemid 10090979)
    • (1980) Biochimica et Biophysica Acta , vol.629 , Issue.2 , pp. 399-408
    • Mazurier, J.1    Spik, G.2
  • 18
    • 0017121183 scopus 로고
    • Comparative circular dichroism studies of iron-free and iron-saturated forms of human serotransferrin and lactotransferrin
    • J. Mazurier, J.-P. Aubert, M.-H. Loucheux-Lefevre, and G. Spik Comparative circular dichroism studies of iron-free and iron-saturated forms of human serotransferrin and lactotransferrin FEBS letters 66 2 1976 238 242
    • (1976) FEBS Letters , vol.66 , Issue.2 , pp. 238-242
    • Mazurier, J.1    Aubert, J.-P.2    Loucheux-Lefevre, M.-H.3    Spik, G.4
  • 19
    • 0000468776 scopus 로고
    • Reporting of objective colour measurements
    • R.G. McGuire Reporting of objective colour measurements Horticultural Science 27 12 1992 1254 1255
    • (1992) Horticultural Science , vol.27 , Issue.12 , pp. 1254-1255
    • McGuire, R.G.1
  • 20
    • 0030719461 scopus 로고    scopus 로고
    • Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
    • DOI 10.1006/jmbi.1997.1386
    • S.A. Moore, B.F. Anderson, C.R. Groom, M. Haridas, and E.N. Baker Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution Journal of Molecular Biology 274 2 1997 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
  • 22
    • 0027765190 scopus 로고
    • Thermal behaviour of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity
    • M.A. Paulsson, U. Svensson, A.R. Kishore, and S. Naidu Thermal behaviour of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity Journal of Dairy Science 76 12 1993 3711 3720
    • (1993) Journal of Dairy Science , vol.76 , Issue.12 , pp. 3711-3720
    • Paulsson, M.A.1    Svensson, U.2    Kishore, A.R.3    Naidu, S.4
  • 23
    • 85054420902 scopus 로고
    • The Australian handbook of soil and water chemical methods
    • G.E. Rayment, and F.R. Higginso The Australian handbook of soil and water chemical methods Inkata Press 1992 36 37
    • (1992) Inkata Press , pp. 36-37
    • Rayment, G.E.1    Higginso, F.R.2
  • 24
    • 84976113450 scopus 로고
    • A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate
    • M. Rüegg, U. Moor, and B. Blanc A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate Journal of Dairy Research 44 03 1977 509 520
    • (1977) Journal of Dairy Research , vol.44 , Issue.3 , pp. 509-520
    • Rüegg, M.1    Moor, U.2    Blanc, B.3
  • 26
    • 0026099978 scopus 로고
    • Comparison of bovine, sheep and goat milk lactoferrins in their electrophoretic behavior, conformation, immunochemical properties and lectin reactivity
    • K.-I. Shimazaki, N. Kawano, and Y.C. Yoo 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 1991 417 422
    • (1991) Comparative Biochemistry and Physiology Part B: Comparative Biochemistry , vol.98 , Issue.23 , pp. 417-422
    • Shimazaki, K.-I.1    Kawano, N.2    Yoo, Y.C.3
  • 27
    • 78349309161 scopus 로고    scopus 로고
    • Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins
    • A. Sreedhara, R. Flengsrud, T. Langsrud, P. Kaul, V. Prakash, and G.E. Vegarud Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins BioMetals 23 6 2010 1159 1170
    • (2010) BioMetals , vol.23 , Issue.6 , pp. 1159-1170
    • Sreedhara, A.1    Flengsrud, R.2    Langsrud, T.3    Kaul, P.4    Prakash, V.5    Vegarud, G.E.6
  • 28
    • 0034492988 scopus 로고    scopus 로고
    • Occurrence, structure, biochemical properties and technological characteristics of lactoferrin
    • J.M. Steijns, and A.C.M. van Hooijdonk Occurrence, structure, biochemical properties and technological characteristics of lactoferrin British Journal of Nutrition 84 SupplementS1 2000 11 17
    • (2000) British Journal of Nutrition , vol.84 , Issue.SUPPL.1 , pp. 11-17
    • Steijns, J.M.1    Van Hooijdonk, A.C.M.2
  • 29
    • 17544364169 scopus 로고    scopus 로고
    • Cooperative interactions between the amino- and carboxyl-terminal lobes contribute to the unique iron-binding stability of lactoferrin
    • DOI 10.1074/jbc.271.22.12790
    • P.P. Ward, X. Zhou, and O.M. Conneely Cooperative interactions between the amino- and carboxyl-terminal lobes contribute to the unique iron-binding stability of lactoferrin The Journal of Biological Chemistry 271 22 1996 12790 12794 (Pubitemid 26175850)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.22 , pp. 12790-12794
    • Ward, P.P.1    Zhou, X.2    Conneely, O.M.3
  • 30
    • 0026785065 scopus 로고
    • Skin colour measurements in terms of CIELAB colour space values
    • I.L. Weatherall, and B.D. Coombs Skin colour measurements in terms of CIELAB colour space values Journal of Investigative Dermatology 99 4 1992 468 473
    • (1992) Journal of Investigative Dermatology , vol.99 , Issue.4 , pp. 468-473
    • Weatherall, I.L.1    Coombs, B.D.2
  • 31
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Academic Press
    • J.T. Yang, C.-S.C. Wu, and H.M. Martinez Calculation of protein conformation from circular dichroism Methods in Enzymology 130 1986 208 269 Academic Press
    • (1986) Methods in Enzymology , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3


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