Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology

FEBS Letters

Volumn 415, Issue 3, 1997, Pages 289-293

  Pedrazzi, Graziella ^a   Schwesinger, Falk ^a   Honegger, Annemarie ^a   Krebber, Claus ^a   Plückthun, Andreas ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Antibody affinity; Antibody engineering; Phage display; Selectively infective phage; Single chain Fv fragment

Indexed keywords

ANTIBODY AFFINITY; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; BINDING SITE; DISSOCIATION CONSTANT; FLUORESCENCE; MUTANT; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; TECHNIQUE;

ANTIBODIES; ANTIBODY AFFINITY; ANTIGEN-ANTIBODY REACTIONS; COLIPHAGES; ESCHERICHIA COLI; FLUORESCEIN-5-ISOTHIOCYANATE; HAPTENS; IMMUNOGLOBULIN FRAGMENTS; IMMUNOGLOBULIN VARIABLE REGION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEPTIDE LIBRARY; PLASMIDS; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE;

EID: 0030869953     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)01143-5     Document Type: Article

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