메뉴 건너뛰기




Volumn 44, Issue 10, 2006, Pages 634-638

Thiophilic interaction chromatography of human transferrins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 33847796177     PISSN: 00219665     EISSN: None     Source Type: Journal    
DOI: 10.1093/chromsci/48.2.634     Document Type: Article
Times cited : (10)

References (32)
  • 2
    • 0343618425 scopus 로고    scopus 로고
    • Inhibition of binding of lactoferrin to the human promonocyte cell line THP-1 by heparin: The role of cell surface sulphated molecules
    • A Rosenau, F. Chelu, M. Trif, C. Motas, and J.H. Brock. Inhibition of binding of lactoferrin to the human promonocyte cell line THP-1 by heparin: the role of cell surface sulphated molecules. Biochim. Biophys. Acta. 1475: 35-38 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1475 , pp. 35-38
    • Rosenau, A.1    Chelu, F.2    Trif, M.3    Motas, C.4    Brock, J.H.5
  • 4
    • 0029012726 scopus 로고
    • Lactoferrin down-modulates the activity of the granulocyte macrophage colony-stimulating factor promoter in interleukin-1 beta-stimulated cells
    • S. Penco, S. Pastorino, G. Bianchi-Scarra, and C Garre. Lactoferrin down-modulates the activity of the granulocyte macrophage colony-stimulating factor promoter in interleukin-1 beta-stimulated cells. J. Biol. Chem. 270: 12263-68 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 12263-12268
    • Penco, S.1    Pastorino, S.2    Bianchi-Scarra, G.3    Garre, C.4
  • 6
    • 0031604903 scopus 로고    scopus 로고
    • The gut. A key metabolic organ protected by lactoferrin during experimental systemic inflammation in mice
    • M.L. Kruzel, Y. Harari, C.Y. Chen, and G.A. Castro. The gut. A key metabolic organ protected by lactoferrin during experimental systemic inflammation in mice. Adv. Exp. Med. Biol. 443: 167-73 (1998).
    • (1998) Adv. Exp. Med. Biol , vol.443 , pp. 167-173
    • Kruzel, M.L.1    Harari, Y.2    Chen, C.Y.3    Castro, G.A.4
  • 9
    • 0027723591 scopus 로고
    • Lactotransferrin immunocytochemistry in Alzheimer and normal human brain
    • T. Kawamata, I. Tooyama, T. Yamada, D.G. Walker, and P.L. McGeer. Lactotransferrin immunocytochemistry in Alzheimer and normal human brain. Amer. J. Pathol. 142: 1574-85 (1993).
    • (1993) Amer. J. Pathol , vol.142 , pp. 1574-1585
    • Kawamata, T.1    Tooyama, I.2    Yamada, T.3    Walker, D.G.4    McGeer, P.L.5
  • 10
    • 0023197325 scopus 로고
    • A one-step purification method for monoclonal antibodies based on salt-promoted adsorption chromatography on a 'thiophilic' adsorbent
    • M. Belew, N. Juntti, A. Larsson, and J. Porath. . A one-step purification method for monoclonal antibodies based on salt-promoted adsorption chromatography on a 'thiophilic' adsorbent. J. Immunol. Methods 102: 173-82 (1987).
    • (1987) J. Immunol. Methods , vol.102 , pp. 173-182
    • Belew, M.1    Juntti, N.2    Larsson, A.3    Porath, J.4
  • 12
    • 0031214161 scopus 로고    scopus 로고
    • Tertiary structural changes and iron release from human serum transferrin
    • S. Mecklenburg, R.J. Donohoe, and G.A. Olah. Tertiary structural changes and iron release from human serum transferrin. J. Mol. Biol. 270: 739-50 (1997).
    • (1997) J. Mol. Biol , vol.270 , pp. 739-750
    • Mecklenburg, S.1    Donohoe, R.J.2    Olah, G.A.3
  • 14
    • 0030598233 scopus 로고    scopus 로고
    • Oxidative-stress associated parameters (lactoferrin, super- oxide dismutases) in serum of patients with Alzheimer's disease
    • J. Thome, W. Gsell, M. Rosler, J. Kornhuber, L. Frolich, E. Hashimoto, B. Zielke, G.A. Wiesbeck, and P. Riederer. . Oxidative-stress associated parameters (lactoferrin, super- oxide dismutases) in serum of patients with Alzheimer's disease. Life Sci. 60: 13-19 (1997).
    • (1997) Life Sci , vol.60 , pp. 13-19
    • Thome, J.1    Gsell, W.2    Rosler, M.3    Kornhuber, J.4    Frolich, L.5    Hashimoto, E.6    Zielke, B.7    Wiesbeck, G.A.8    Riederer, P.9
  • 15
    • 45949124114 scopus 로고
    • Purification of transferrins and lactoferrin using DEAE affi-gel blue
    • M. Chung Ching-Ming, Chan, Siew-Lee, S. Shimazu. Purification of transferrins and lactoferrin using DEAE affi-gel blue. Int. J. Biochem. 23: 609-16 (1991).
    • (1991) Int. J. Biochem , vol.23 , pp. 609-616
    • Chung Ching-Ming, M.1    Chan2    Siew-Lee3    Shimazu, S.4
  • 16
    • 28844498598 scopus 로고    scopus 로고
    • Purification of transferrin from Cohn supernatant I using ion-exchange chromatography
    • K.B. McCann, B. Hughes, J. Wu, J. Bertolini, P.T. Gomme. Purification of transferrin from Cohn supernatant I using ion-exchange chromatography. Biotechnol. Appl. Biochem. 42: 211-17 (2005).
    • (2005) Biotechnol. Appl. Biochem , vol.42 , pp. 211-217
    • McCann, K.B.1    Hughes, B.2    Wu, J.3    Bertolini, J.4    Gomme, P.T.5
  • 17
    • 0021832928 scopus 로고
    • Thiophilic adsorption - a new method for protein fractionation
    • J. Porath, F. Maisano, and M. Belew. Thiophilic adsorption - a new method for protein fractionation. FEBS Lett. 185: 306-10 (1985).
    • (1985) FEBS Lett , vol.185 , pp. 306-310
    • Porath, J.1    Maisano, F.2    Belew, M.3
  • 18
    • 0023643397 scopus 로고
    • Thiophilic adsorption: A comparison of model protein behavior
    • T.W. Hutchens and J. Porath. Thiophilic adsorption: a comparison of model protein behavior. Biochemistry 26: 7199-7204 (1987).
    • (1987) Biochemistry , vol.26 , pp. 7199-7204
    • Hutchens, T.W.1    Porath, J.2
  • 20
    • 0025967968 scopus 로고
    • Thiophilic adsorption chromatography: The separation of serum proteins
    • A. Lihme and M.H. Heegaard. Thiophilic adsorption chromatography: the separation of serum proteins. Anal. Biochem, 192: 64-69 (1990).
    • (1990) Anal. Biochem , vol.192 , pp. 64-69
    • Lihme, A.1    Heegaard, M.H.2
  • 21
    • 0033371505 scopus 로고    scopus 로고
    • Thiophilic interaction chromatography: Principles and applications
    • H.G. Botros. Thiophilic interaction chromatography: Principles and applications. Int. J. Biol. Chem. 4: 209-20 (1999).
    • (1999) Int. J. Biol. Chem , vol.4 , pp. 209-220
    • Botros, H.G.1
  • 22
    • 0023399231 scopus 로고
    • Thiophilic' interaction and the selective adsorption of proteins
    • J. Porath, F. Maisano, and M. Belew. Thiophilic' interaction and the selective adsorption of proteins. Trends Biotechnol. 5: 225-29 (1985).
    • (1985) Trends Biotechnol , vol.5 , pp. 225-229
    • Porath, J.1    Maisano, F.2    Belew, M.3
  • 23
    • 0035975904 scopus 로고    scopus 로고
    • The use of thiophilic chromatography for antibody purification: A review
    • E. Boschetti. The use of thiophilic chromatography for antibody purification: a review. J. Biochem. Biophys. Methods. 49: 361-89 (2001).
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 361-389
    • Boschetti, E.1
  • 24
    • 0035946746 scopus 로고    scopus 로고
    • Thiophilic interaction chromatography of prostate-specific antigen
    • K.C. Chadha, E. Kawinski, and E. Sulkowski. Thiophilic interaction chromatography of prostate-specific antigen. J. Chromatogr. B 754: 521-25 (2001).
    • (2001) J. Chromatogr. B , vol.754 , pp. 521-525
    • Chadha, K.C.1    Kawinski, E.2    Sulkowski, E.3
  • 26
    • 33645086629 scopus 로고    scopus 로고
    • Thiophilic intertaction chromatography of Alzheimer's β-amyloid peptides
    • S. Perry, D. Todorova-Balvay, T. Srikrishnan, and E. Sulkowski. Thiophilic intertaction chromatography of Alzheimer's β-amyloid peptides. J. Pep. Res. (Suppl. 1) 99-105 (2006).
    • (2006) J. Pep. Res , Issue.SUPPL. 1 , pp. 99-105
    • Perry, S.1    Todorova-Balvay, D.2    Srikrishnan, T.3    Sulkowski, E.4
  • 27
    • 0026664020 scopus 로고
    • Hydrophobic charge induction chromatography: Salt independent protein adsorption and facile elution with aqueous buffers
    • C.A. Smith, B.F. Anderson, H.M. Baker, and E.N. Baker. Hydrophobic charge induction chromatography: salt independent protein adsorption and facile elution with aqueous buffers. Biochem. 31: 4527-33 (1992).
    • (1992) Biochem , vol.31 , pp. 4527-4533
    • Smith, C.A.1    Anderson, B.F.2    Baker, H.M.3    Baker, E.N.4
  • 29
    • 0031858337 scopus 로고    scopus 로고
    • Hydrophobic charge induction chromatography: Salt independent protein adsorption and facile elution with aqueous buffers
    • S.C. Burton and D.R.K. Harding. Hydrophobic charge induction chromatography: salt independent protein adsorption and facile elution with aqueous buffers. J. Chromatogr. A 814: 71-81 (1998).
    • (1998) J. Chromatogr. A , vol.814 , pp. 71-81
    • Burton, S.C.1    Harding, D.R.K.2
  • 30
    • 0029130333 scopus 로고
    • Lactoferrin: Molecular structure and biological function
    • B. Lonnerdal, and S. Iyer. Lactoferrin: molecular structure and biological function. Annu. Rev. Nutr. 15: 93-110 (1995).
    • (1995) Annu. Rev. Nutr , vol.15 , pp. 93-110
    • Lonnerdal, B.1    Iyer, S.2
  • 31


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.