Bacteriophage lambda surface display of a bacterial biotin acceptor domain reveals the minimal peptide size required for biotinylation

FEBS Letters

Volumn 440, Issue 1-2, 1998, Pages 213-217

  Stolz, Jürgen ^a   Ludwig, Andreas ^a   Sauer, Norbert ^a  

^a UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

Bacteriophage lambda; Biotin; Enzymatic biotinylation; Phage display

Indexed keywords

BIOTIN;

ARTICLE; BACTERIOPHAGE LAMBDA; BIOTINYLATION; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; AVIDIN; BACTERIAL PROTEINS; BACTERIOPHAGE LAMBDA; BINDING SITES; BIOTIN; BIOTINYLATION; BLOTTING, WESTERN; CARBOXY-LYASES; CHROMATOGRAPHY, AFFINITY; CLONING, MOLECULAR; KLEBSIELLA PNEUMONIAE; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY; PEPTIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA;

BACTERIA (MICROORGANISMS); BACTERIOPHAGE LAMBDA; KLEBSIELLA PNEUMONIAE;

EID: 0032573515     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)01454-9     Document Type: Article

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