메뉴 건너뛰기




Volumn 103, Issue 1, 2011, Pages 41-47

Calorimetric and Raman investigation of cow's milk lactoferrin

Author keywords

Differential scanning calorimetry; Lactoferrin; Protein biophysics; Protein denaturation; Raman spectroscopy

Indexed keywords

AFTER-HEAT; ANTI-INFLAMMATORIES; BLOOD PLASMA; DENATURATION TEMPERATURES; DSC CURVES; ENTHALPY CHANGE; HEME IRON; LACTOFERRIN; PH VARIATION; PHYSIOLOGICAL PH; PROTEIN DENATURATION; PROTEIN SOLUTION; RAMAN INVESTIGATIONS; SECONDARY STRUCTURES; SPECTROSCOPIC INVESTIGATIONS; THERMAL STABILITY; TURN STRUCTURE; WIDE PH RANGE;

EID: 79951477786     PISSN: 13886150     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10973-010-1084-2     Document Type: Conference Paper
Times cited : (19)

References (24)
  • 1
    • 0021677758 scopus 로고
    • Human lactotransferrin: Amino acid sequence and structural comparisons with other transferrins
    • DOI 10.1111/j.1432-1033.1984.tb08607.x
    • MH Metz-Boutique J Jolles J Mazurier F Schoentgen D Legrand G Spik J Montreuil P Jolles 1984 Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins Eur J Biochem. 145 659 676 10.1111/j.1432-1033.1984.tb08607.x (Pubitemid 15178137)
    • (1984) European Journal of Biochemistry , vol.145 , Issue.3 , pp. 659-676
    • Metz-Boutigue, M.-H.1    Jolles, J.2    Mazurier, J.3
  • 2
    • 0034492988 scopus 로고    scopus 로고
    • Occurrence structure biochemical properties and technological characteristics of lactoferrin
    • 10.1017/S0007114500002191
    • JM Steijns ACM Van Hooijdonk 2000 Occurrence structure biochemical properties and technological characteristics of lactoferrin Br J Nutr. 84 11 17 10.1017/S0007114500002191
    • (2000) Br J Nutr. , vol.84 , pp. 11-17
    • Steijns, J.M.1    Van Hooijdonk, A.C.M.2
  • 3
    • 77950851910 scopus 로고    scopus 로고
    • A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin
    • 1:CAS:528:DC%2BC3cXkvFKkurk%3D 10.1016/j.idairyj.2010.02.003
    • A Sreedhara R Flengsrud V Prakash D Krowarsch T Langsrud P Kaul TG Devold GE Vegarud 2010 A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin Int Dairy J. 20 487 494 1:CAS:528:DC%2BC3cXkvFKkurk%3D 10.1016/j.idairyj.2010.02.003
    • (2010) Int Dairy J. , vol.20 , pp. 487-494
    • Sreedhara, A.1    Flengsrud, R.2    Prakash, V.3    Krowarsch, D.4    Langsrud, T.5    Kaul, P.6    Devold, T.G.7    Vegarud, G.E.8
  • 4
    • 0032213139 scopus 로고    scopus 로고
    • Structure of human apolactoferrin at 2.0 Å resolution. Refinement and analysis of ligand induced conformational change
    • DOI 10.1107/S0907444998004417
    • GB Jameson BF Anderson GE Norris DH Thomas EN Baker 1998 Structure of human apolactoferrin at 2.0 Å resolution. refinement and analysis of ligand-induced conformational change Acta Crystallogr D Biol Crystallogr. 54 1319 1335 1:STN:280:DyaK1M7pt1KktQ%3D%3D 10.1107/S0907444998004417 (Pubitemid 28560409)
    • (1998) Acta Crystallographica Section D: Biological Crystallography , vol.54 , Issue.6 II , pp. 1319-1335
    • Jameson, G.B.1    Anderson, B.F.2    Norris, G.E.3    Thomas, D.H.4    Baker, E.N.5
  • 5
    • 28344440468 scopus 로고    scopus 로고
    • Molecular structure, binding properties and dynamics of lactoferrin
    • DOI 10.1007/s00018-005-5368-9
    • EN Baker HM Baker 2005 Molecular structure, binding properties and dynamics of lactoferrin Cell Mol Life Sci. 62 2531 2539 1:CAS:528: DC%2BD2MXhtlSms7rE 10.1007/s00018-005-5368-9 (Pubitemid 41721228)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2531-2539
    • Baker, E.N.1    Baker, H.M.2
  • 7
    • 41549150181 scopus 로고    scopus 로고
    • Isolation of lactoferrin from milk of different species: Calorimetric and antimicrobial studies
    • 10.1016/j.cbpb.2008.02.005
    • C Conesa L Sánchez C Rota MD Pérez M Calvo S Farnaud RW Evans 2008 Isolation of lactoferrin from milk of different species: calorimetric and antimicrobial studies Comp Biochem Physiol Part B. 150 131 139 10.1016/j.cbpb.2008.02.005
    • (2008) Comp Biochem Physiol Part B. , vol.150 , pp. 131-139
    • Conesa, C.1    Sánchez, L.2    Rota, C.3    Pérez, M.D.4    Calvo, M.5    Farnaud, S.6    Evans, R.W.7
  • 9
    • 84976113450 scopus 로고
    • A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate
    • 10.1017/S002202990002046X
    • M Rüegg U Moor B Blanc 1977 A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate J Dairy Res. 44 509 520 10.1017/S002202990002046X
    • (1977) J Dairy Res. , vol.44 , pp. 509-520
    • Rüegg, M.1    Moor, U.2    Blanc, B.3
  • 10
    • 84987350883 scopus 로고
    • Kinetic parameters for denaturation of bovine milk lactoferrin
    • 10.1111/j.1365-2621.1992.tb14313.x
    • L Sánchez JM Peiró H Castillo MD Pérez J Ena M Calvo 1992 Kinetic parameters for denaturation of bovine milk lactoferrin J Food Sci. 57 873 879 10.1111/j.1365-2621.1992.tb14313.x
    • (1992) J Food Sci. , vol.57 , pp. 873-879
    • Sánchez, L.1    Peiró, J.M.2    Castillo, H.3    Pérez, M.D.4    Ena, J.5    Calvo, M.6
  • 11
    • 55249101197 scopus 로고    scopus 로고
    • Effect of sulfoxides on the thermal denaturation of hen lysozyme: A calorimetric and Raman study
    • 1:CAS:528:DC%2BD1cXhtlOhsLfL 10.1016/j.molstruc.2008.03.007
    • A Torreggiani M Di Foggia I Manco A De Maio SA Markarian S Bonora 2008 Effect of sulfoxides on the thermal denaturation of hen lysozyme: a calorimetric and Raman study J Mol Struct. 891 115 122 1:CAS:528:DC%2BD1cXhtlOhsLfL 10.1016/j.molstruc.2008.03.007
    • (2008) J Mol Struct. , vol.891 , pp. 115-122
    • Torreggiani, A.1    Di Foggia, M.2    Manco, I.3    De Maio, A.4    Markarian, S.A.5    Bonora, S.6
  • 12
    • 0039163193 scopus 로고
    • Applications of scanning calorimetry to the study of protein behaviour in foods
    • B.J.F. Hudson (eds). Applied Science Publishers London, England
    • Wright DJ. Applications of scanning calorimetry to the study of protein behaviour in foods. In: Hudson BJF, editor. Developments in food proteins-1. London, England: Applied Science Publishers; 1982.
    • (1982) Developments in Food proteins-1
    • Wright, D.J.1
  • 13
    • 38249015088 scopus 로고
    • Effect of ionic strength and pH on the thermostability of lactoferrin
    • 1:CAS:528:DyaK3sXlvVOl 10.1016/0958-6946(92)90033-I
    • H Kawakami M Tanaka K Tatsumi S Dosako 1992 Effect of ionic strength and pH on the thermostability of lactoferrin Int Dairy J. 2 287 298 1:CAS:528:DyaK3sXlvVOl 10.1016/0958-6946(92)90033-I
    • (1992) Int Dairy J. , vol.2 , pp. 287-298
    • Kawakami, H.1    Tanaka, M.2    Tatsumi, K.3    Dosako, S.4
  • 14
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • 1:CAS:528:DyaL3sXkvVOlug%3D%3D 10.1016/S0065-3233(08)60468-4
    • PL Privalov 1982 Stability of proteins. Proteins which do not present a single cooperative system Adv Protein Chem. 35 1 104 1:CAS:528: DyaL3sXkvVOlug%3D%3D 10.1016/S0065-3233(08)60468-4
    • (1982) Adv Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 15
    • 0542369596 scopus 로고    scopus 로고
    • Thermal Denaturation of Human Lactoferrin and Its Effect on the Ability to Bind Iron
    • L Mata L Sánchez DR Headon M Calvo 1998 Thermal denaturation of human lactoferrin and its effect on the ability to bind iron J Agric Food Chem. 46 3964 3970 1:CAS:528:DyaK1cXmtV2gtbg%3D 10.1021/jf980266d (Pubitemid 128488477)
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.10 , pp. 3964-3970
    • Mata, L.1    Sanchez, L.2    Headon, D.R.3    Calvo, M.4
  • 16
    • 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
    • BF Anderson HM Baker GE Norris DW Rice EN Baker 1989 Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 Å resolution J Mol Biol. 209 711 734 1:CAS:528:DyaK3cXltVOitQ%3D%3D 10.1016/0022-2836(89)90602-5 (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
  • 17
    • 0018139236 scopus 로고
    • Studies of the binding of different iron donors to human serum transferrin and isolation of iron binding fragments from the N and C terminal regions of the protein
    • RW Evans J Williams 1978 Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C-terminal regions of the protein Biochem J. 173 543 552 1:CAS:528:DyaE1MXot1Cjsg%3D%3D (Pubitemid 8395171)
    • (1978) Biochemical Journal , vol.173 , Issue.2 , pp. 543-552
    • Evans, R.W.1    Williams, J.2
  • 18
    • 34250691405 scopus 로고    scopus 로고
    • A calorimetric study of thermal denaturation of recombinant human lactoferrin from rice
    • DOI 10.1021/jf063335u
    • C Conesa L Sanchez MD Perez M Calvo 2007 A calorimetric study of thermal denaturation of recombinant human lactoferrin from rice J Agric Food Chem. 55 4848 4853 1:CAS:528:DC%2BD2sXlt1Ogtro%3D 10.1021/jf063335u (Pubitemid 46960915)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.12 , pp. 4848-4853
    • Conesa, C.1    Sanchez, L.2    Perez, M.-D.3    Calvo, M.4
  • 19
    • 0002660213 scopus 로고
    • Peptide backbone conformation and microenvironment of protein side-chains
    • Clark RJ, Hester RE, editors Chichester: Wiley
    • Tu A. Peptide backbone conformation and microenvironment of protein side-chains. In: Clark RJ, Hester RE, editors. Spectroscopy of biological systems. vol 13. Chichester: Wiley: (1986). pp. 47-112.
    • (1986) Spectroscopy of Biological Systems , vol.13 , pp. 47-112
    • Tu, A.1
  • 20
    • 0001021914 scopus 로고    scopus 로고
    • Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman Amide i band
    • 10.1016/0022-2860(88)80151-0
    • AJP Alix G Pedanou M Berjot 1998 Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman Amide I band J Mol Struct. 174 159 164 10.1016/0022-2860(88)80151-0
    • (1998) J Mol Struct. , vol.174 , pp. 159-164
    • Alix, A.J.P.1    Pedanou, G.2    Berjot, M.3
  • 21
    • 0024284778 scopus 로고    scopus 로고
    • Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics
    • 10.1021/bi00401a015
    • T Miura H Takeuchi I Harada 1998 Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics Biochemistry. 27 88 94 10.1021/bi00401a015
    • (1998) Biochemistry. , vol.27 , pp. 88-94
    • Miura, T.1    Takeuchi, H.2    Harada, I.3
  • 22
    • 84988158466 scopus 로고
    • Tryptophan Raman bands sensitive to hydrogen bonding and side-chain conformation
    • 1:CAS:528:DyaK3cXhtlGltg%3D%3D 10.1002/jrs.1250201007
    • T Miura H Takeuchi I Harada 1989 Tryptophan Raman bands sensitive to hydrogen bonding and side-chain conformation J Raman Spectrosc. 20 667 671 1:CAS:528:DyaK3cXhtlGltg%3D%3D 10.1002/jrs.1250201007
    • (1989) J Raman Spectrosc. , vol.20 , pp. 667-671
    • Miura, T.1    Takeuchi, H.2    Harada, I.3
  • 23
    • 0019218291 scopus 로고
    • Studies on human lactoferrin by electron paramagnetic resonance, fluorescence, and resonance raman spectroscopy
    • DOI 10.1021/bi00558a026
    • EW Ainscough AM Brodie JE Plowman SJ Bloor JS Loehr TM Loehr 1980 Studies on human lactoferrin by electron paramagnetic resonance, fluorescence, and resonance Raman spectroscopy Biochemistry. 19 4072 4079 1:CAS:528: DyaL3cXlsVCqsLg%3D 10.1021/bi00558a026 (Pubitemid 11242467)
    • (1980) Biochemistry , vol.19 , Issue.17 , pp. 4072-4079
    • Ainscough, E.W.1    Brodie, A.M.2    Plowman, J.E.3
  • 24
    • 0017104275 scopus 로고
    • Resonance Raman spectra of iron(III)-, copper(II)-, cobalt(III)-, and manganese(III)-transferrins and of bis(2,4,6-trichlorophenolato) diimidazolecopper(II) monohydrate, a possible model for copper(II) binding to transferrins
    • 1:CAS:528:DyaE28XlvVyjtLs%3D 10.1021/bi00667a026
    • Y Tomimatsu S Kint JR Scherer 1976 Resonance Raman spectra of iron(III)-, copper(II)-, cobalt(III)-, and manganese(III)-transferrins and of bis(2,4,6-trichlorophenolato)diimidazolecopper(II) monohydrate, a possible model for copper(II) binding to transferrins Biochemistry. 15 4918 4924 1:CAS:528:DyaE28XlvVyjtLs%3D 10.1021/bi00667a026
    • (1976) Biochemistry. , vol.15 , pp. 4918-4924
    • Tomimatsu, Y.1    Kint, S.2    Scherer, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.