Hydrophobic sequences can substitute for the wild-type N-terminal sequence of cystatin A (stefin A) in tight binding to cysteine proteinases. Selection of high-affinity N-terminal region variants by phage display

European Journal of Biochemistry

Volumn 261, Issue 3, 1999, Pages 682-688

  Ylinenjärvi, Karin ^b   Widersten, Mikael ^b   Björk, Ingemar ^a  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b NONE

Author keywords

Cystatin; Cysteine protease; Cysteine protease inhibitor; N terminal sequence; Phage display

Indexed keywords

CATHEPSIN B; CYSTATIN; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; PAPAIN; STEFIN A;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; DISSOCIATION CONSTANT; ENZYME INHIBITOR INTERACTION; EQUILIBRIUM CONSTANT; HYDROPHOBICITY; PHAGE DISPLAY; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; BACTERIOPHAGES; BASE SEQUENCE; CYSTATINS; CYSTEINE ENDOPEPTIDASES; DNA PRIMERS; KINETICS; PROTEIN BINDING;

EID: 0006513086     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00312.x     Document Type: Article

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