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Volumn 84, Issue 1 C, 2006, Pages 3-8

Affilin™ molecules: Novel ligands for bioseparation

Author keywords

Affilin ; Affinity chromatography; Bioseparation; ProNGF; B crystallin

Indexed keywords

AFFINITY CHROMATOGRAPHY; BIOCHEMISTRY; CHARACTERIZATION; MOLECULES; PROTEINS; PURIFICATION; SEPARATION; SURFACE PLASMON RESONANCE;

EID: 33646581375     PISSN: 09603085     EISSN: None     Source Type: Journal    
DOI: 10.1205/fbp.05222     Document Type: Article
Times cited : (9)

References (20)
  • 1
    • 0008724932 scopus 로고    scopus 로고
    • BIAcore AB, Uppsala, Sweden
    • BIAapplications Handbook, 1998, BIAcore AB, Uppsala, Sweden.
    • (1998) BIAapplications Handbook
  • 2
    • 0036669677 scopus 로고    scopus 로고
    • Advances in gentle immunoaffinity chromatography
    • Burgess, R.R. and Thompson, N.E., 2002, Advances in gentle immunoaffinity chromatography, Curr Opin Biotechnol, 13(4): 304-308.
    • (2002) Curr Opin Biotechnol , vol.13 , Issue.4 , pp. 304-308
    • Burgess, R.R.1    Thompson, N.E.2
  • 5
    • 33646568632 scopus 로고    scopus 로고
    • Monoclonal antibodies used as reagent in drug manufacturing
    • FDA Guidance for Industry
    • FDA Guidance for Industry, 2001, Monoclonal antibodies used as reagent in drug manufacturing, http://www.fda.gov/cder/guidance/3630fnl.pdf.
    • (2001)
  • 7
    • 0032895673 scopus 로고    scopus 로고
    • Affinity chromatography: A review of clinical applications
    • Hage, D.S., 1999, Affinity chromatography: A review of clinical applications, Clin Chem, 45: 593-615.
    • (1999) Clin Chem , vol.45 , pp. 593-615
    • Hage, D.S.1
  • 8
    • 0343314905 scopus 로고    scopus 로고
    • Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris
    • Hardy, E., Martinez, E., Diago, D., Diaz, R., Gonzalez, D. and Herrera, L., 2000, Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris, J Biotechnol, 77: 157-167.
    • (2000) J Biotechnol , vol.77 , pp. 157-167
    • Hardy, E.1    Martinez, E.2    Diago, D.3    Diaz, R.4    Gonzalez, D.5    Herrera, L.6
  • 9
    • 24944450680 scopus 로고    scopus 로고
    • Artificial, non-antibody binding proteins for pharmaceutical and industrial applications
    • Hey, T., Fiedler, E., Rudolph, R. and Fiedler, M., 2005, Artificial, non-antibody binding proteins for pharmaceutical and industrial applications, Trends in Biotechnol, 23(10): 514-522.
    • (2005) Trends in Biotechnol , vol.23 , Issue.10 , pp. 514-522
    • Hey, T.1    Fiedler, E.2    Rudolph, R.3    Fiedler, M.4
  • 10
    • 0028104494 scopus 로고
    • Eye-lens proteins: Structure, superstructure, stability, genetics
    • Jaenicke, R., 1994, Eye-lens proteins: structure, superstructure, stability, genetics, Naturwissenschaften, 81: 423-429.
    • (1994) Naturwissenschaften , vol.81 , pp. 423-429
    • Jaenicke, R.1
  • 11
    • 0030067190 scopus 로고    scopus 로고
    • Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles
    • Jaenicke, R., 1996, Stability and folding of ultrastable proteins: eye lens crystallins and enzymes from thermophiles, Faseb J, 10: 84-92.
    • (1996) Faseb J , vol.10 , pp. 84-92
    • Jaenicke, R.1
  • 12
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: Structure, stability, and function
    • Jaenicke, R. and Slingsby, C., 2001, Lens crystallins and their microbial homologs: structure, stability, and function, Crit Rev Biochem Mol Biol, 36: 435-499.
    • (2001) Crit Rev Biochem Mol Biol , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 14
    • 3142677981 scopus 로고    scopus 로고
    • Binding proteins from alternative scaffolds
    • Nygren, P.A. and Skerra, A., 2004, Binding proteins from alternative scaffolds, J Immunol Methods, 290: 3-28.
    • (2004) J Immunol Methods , vol.290 , pp. 3-28
    • Nygren, P.A.1    Skerra, A.2
  • 15
    • 0034851615 scopus 로고    scopus 로고
    • The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies
    • Rattenholl, A., Lilie, H., Grossmann, A., Stern, A., Schwarz, E. and Rudolph, R., 2001, The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies. Eur J Biochem 268: 3296-3303.
    • (2001) Eur J Biochem , vol.268 , pp. 3296-3303
    • Rattenholl, A.1    Lilie, H.2    Grossmann, A.3    Stern, A.4    Schwarz, E.5    Rudolph, R.6
  • 16
    • 0025339471 scopus 로고
    • Folding of an all-beta protein: Independent domain folding in gamma II-crystallin from calf eye lens
    • Rudolph, R., Siebendritt, R., Nesslauer, G., Sharma, A.K. and Jaenicke, R., 1990, Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens, Proc Natl Acad Sci, 87: 4625-4629.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 4625-4629
    • Rudolph, R.1    Siebendritt, R.2    Nesslauer, G.3    Sharma, A.K.4    Jaenicke, R.5
  • 17
    • 0019304419 scopus 로고
    • A monoclonal antibody for large-scale purification of human leukocyte interferon
    • Secher, D.S. and Burke, D.C., 1980, A monoclonal antibody for large-scale purification of human leukocyte interferon, Nature, 285(5765): 446-450.
    • (1980) Nature , vol.285 , Issue.5765 , pp. 446-450
    • Secher, D.S.1    Burke, D.C.2
  • 18
    • 0025670590 scopus 로고
    • Limited proteolysis of gamma II-crystallin from calf eye lens. Physicochemical studies on the N-terminal domain and the intact two-domain protein
    • Sharma, A.K., Minke-Gogl, V., Gohl, P., Siebendritt, R., Jaenicke, R. and Rudolph, R., 1990, Limited proteolysis of gamma II-crystallin from calf eye lens. Physicochemical studies on the N-terminal domain and the intact two-domain protein, Eur J Biochem, 194: 603-609.
    • (1990) Eur J Biochem , vol.194 , pp. 603-609
    • Sharma, A.K.1    Minke-Gogl, V.2    Gohl, P.3    Siebendritt, R.4    Jaenicke, R.5    Rudolph, R.6
  • 19
    • 0344033650 scopus 로고    scopus 로고
    • Imitating the humoral immune response
    • Skerra, A., 2003, Imitating the humoral immune response, Curr Opin Chem Biol, 7: 683-693.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 683-693
    • Skerra, A.1
  • 20
    • 0036155277 scopus 로고    scopus 로고
    • Immunoaffinity chromatography
    • Subramanian, A., 2002, Immunoaffinity chromatography, Mol Biotechnol, 20: 41-47.
    • (2002) Mol Biotechnol , vol.20 , pp. 41-47
    • Subramanian, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.