Discriminating between the activities of human cathepsin G and chymase using fluorogenic substrates

FEBS Journal

Volumn 278, Issue 15, 2011, Pages 2635-2646

  Korkmaz, Brice ^a   Jégot, Gwenhael ^a   Lau, Laurie C ^b   Thorpe, Michael ^c   Pitois, Elodie ^a   Juliano, Luiz ^d   Walls, Andrew F ^b   Hellman, Lars ^c   Gauthier, Francis ^a  

^a UNIVERSITÉ DE TOURS   (France)

^b SOUTHAMPTON GENERAL HOSPITAL   (United Kingdom)

^c UPPSALA UNIVERSITY   (Sweden)

^d FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

cathepsin G; chymase; FRET substrate; kinetics; mast cell; serine protease

Indexed keywords

CATHEPSIN G; CHYMASE; TRYPTASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ASTHMA; CELL FREE SYSTEM; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DEGRADATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROPHILICITY; INFLAMMATORY DISEASE; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; SPUTUM;

BINDING SITES; CATHEPSIN G; CELL LINE; CHYMASES; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; HUMANS; MAST CELLS; MODELS, MOLECULAR; OLIGOPEPTIDES; SUBSTRATE SPECIFICITY;

EID: 79960577818     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08189.x     Document Type: Article

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