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Volumn 118, Issue 2, 2007, Pages 97-103

Calorimetric study of nonspecific interaction between lead ions and bovine serum albumin

Author keywords

Binding; Calorimetry; Enthalpy; Lead ion; Titration

Indexed keywords

BOVINE SERUM ALBUMIN; LEAD;

EID: 34948850263     PISSN: 01634984     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12011-007-0001-4     Document Type: Article
Times cited : (9)

References (17)
  • 1
    • 0027943670 scopus 로고
    • Zinc(II) and copper(II) binding to serum albumin. A comparative study of dog, bovine, and human albumin
    • Masuoka J, Saltman P (1994) Zinc(II) and copper(II) binding to serum albumin. A comparative study of dog, bovine, and human albumin. J Biol Chem 269(41):25557-25561
    • (1994) J Biol Chem , vol.269 , Issue.41 , pp. 25557-25561
    • Masuoka, J.1    Saltman, P.2
  • 3
    • 23844471367 scopus 로고    scopus 로고
    • Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine
    • Hu Y, Liu Y, Jiang W et al (2005) Fluorometric investigation of the interaction of bovine serum albumin with surfactants and 6-mercaptopurine. J Photochem Photobiol B 80:235-242
    • (2005) J Photochem Photobiol B , vol.80 , pp. 235-242
    • Hu, Y.1    Liu, Y.2    Jiang, W.3
  • 4
    • 0025604724 scopus 로고
    • Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and frit-FAB LC/MS
    • Hirayama K, Akashi S, Furuya M, Fukuhara KI (1990) Rapid confirmation and revision of the primary structure of bovine serum albumin by ESIMS and frit-FAB LC/MS. Biochem Biophys Res Commun 173:639-646
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 639-646
    • Hirayama, K.1    Akashi, S.2    Furuya, M.3    Fukuhara, K.I.4
  • 5
    • 0021782306 scopus 로고
    • Serum albumin
    • Peters T (1985) Serum albumin. Adv Protein Chem 37:161-245
    • (1985) Adv Protein Chem , vol.37 , pp. 161-245
    • Peters, T.1
  • 7
    • 0043032426 scopus 로고    scopus 로고
    • Unfolding of rabbit muscle creatine kinase induced by acid: A study using electrospray ionization mass spectrometry, isothermal titration calorimetry, and fluorescence spectroscopy
    • Liang Y, Du F, Sanglier S et al (2003) Unfolding of rabbit muscle creatine kinase induced by acid: a study using electrospray ionization mass spectrometry, isothermal titration calorimetry, and fluorescence spectroscopy. J Biol Chem 278:30098-30105
    • (2003) J Biol Chem , vol.278 , pp. 30098-30105
    • Liang, Y.1    Du, F.2    Sanglier, S.3
  • 8
    • 6344287900 scopus 로고    scopus 로고
    • Micellization of cationic gemini surfactants with various counterions and their interaction with DNA in aqueous solution
    • Jiang N, Li P, Wang Y et al (2004) Micellization of cationic gemini surfactants with various counterions and their interaction with DNA in aqueous solution. J Phys Chem B 108:15385-15391
    • (2004) J Phys Chem B , vol.108 , pp. 15385-15391
    • Jiang, N.1    Li, P.2    Wang, Y.3
  • 9
    • 13844276033 scopus 로고    scopus 로고
    • Analysis of the interactions between human serum albumin/ amphiphilic penicillin in different aqueous media: An isothermal titration calorimetry and dynamic light scattering study
    • Barbosa S, Taboada P, Mosquera V (2005) Analysis of the interactions between human serum albumin/ amphiphilic penicillin in different aqueous media: an isothermal titration calorimetry and dynamic light scattering study. Chem Phys 310:51-58
    • (2005) Chem Phys , vol.310 , pp. 51-58
    • Barbosa, S.1    Taboada, P.2    Mosquera, V.3
  • 10
    • 34247402265 scopus 로고    scopus 로고
    • The application of isothermal microcalorimetry in life science research
    • Peng L, Yi L, Yougui C, Songsheng Q (2002) The application of isothermal microcalorimetry in life science research. HuaXueTongbao 10:682-688
    • (2002) HuaXueTongbao , vol.10 , pp. 682-688
    • Peng, L.1    Yi, L.2    Yougui, C.3    Songsheng, Q.4
  • 11
    • 0142042836 scopus 로고    scopus 로고
    • The physicochemical properties and antitumor activity of cellulase-treated chitosan
    • Caiqin Q, Bo Z, Lintao Z et al (2004) The physicochemical properties and antitumor activity of cellulase-treated chitosan. Food Chem 84(1):107-115
    • (2004) Food Chem , vol.84 , Issue.1 , pp. 107-115
    • Caiqin, Q.1    Bo, Z.2    Lintao, Z.3
  • 12
    • 0036192315 scopus 로고    scopus 로고
    • Thermodynamics of binding of cadmium to bovine serum albumin
    • Songsheng Qu, Yi L, Tianzhi W et al (2002) Thermodynamics of binding of cadmium to bovine serum albumin. Chemosphere 46(8):1211-1214
    • (2002) Chemosphere , vol.46 , Issue.8 , pp. 1211-1214
    • Songsheng, Q.1    Yi, L.2    Tianzhi, W.3
  • 13
    • 0000351667 scopus 로고    scopus 로고
    • Interaction between bovine serum albumin and saponin as studied by heat stability and protease digestion
    • Ikedo S, Shimoyamada M, Watanabe KJ (1996) Interaction between bovine serum albumin and saponin as studied by heat stability and protease digestion. J Agric Food Chem 44:792-795
    • (1996) J Agric Food Chem , vol.44 , pp. 792-795
    • Ikedo, S.1    Shimoyamada, M.2    Watanabe, K.J.3
  • 14
    • 27444432790 scopus 로고    scopus 로고
    • Kinetic analysis of metal binding to the amino-terminal domain of ZntA by monitoring metal-thiolate charge-transfer complexes
    • Dutta SJ, Liu J, Mitra B (2005) Kinetic analysis of metal binding to the amino-terminal domain of ZntA by monitoring metal-thiolate charge-transfer complexes. Biochemistry 44(43):14268-14274
    • (2005) Biochemistry , vol.44 , Issue.43 , pp. 14268-14274
    • Dutta, S.J.1    Liu, J.2    Mitra, B.3
  • 16
    • 3142665600 scopus 로고    scopus 로고
    • Binding of lead ion to bovine serum albumin studied by ion selective electrode
    • Ayranci D (2004) Binding of lead ion to bovine serum albumin studied by ion selective electrode. Protein Pept Lett 11(4):331-337
    • (2004) Protein Pept Lett , vol.11 , Issue.4 , pp. 331-337
    • Ayranci, D.1
  • 17
    • 25844527128 scopus 로고    scopus 로고
    • Quantifying Pb and Cd complexation by alginates and the role of metal binding on macromolecular aggregation
    • Lamelas C, Avaltroni F, Benedetti M et al (2005) Quantifying Pb and Cd complexation by alginates and the role of metal binding on macromolecular aggregation. Biomacromolecules 6(5):2756-2764
    • (2005) Biomacromolecules , vol.6 , Issue.5 , pp. 2756-2764
    • Lamelas, C.1    Avaltroni, F.2    Benedetti, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.