Cathepsin B carboxydipeptidase specificity analysis using internally quenched fluorescent peptides

Biochemical Journal

Volumn 368, Issue 1, 2002, Pages 365-369

  Cezari, Maria Helena S ^a   Puzer, Luciano ^a   Juliano, Maria Aparecida ^a   Carmona, Adriana K ^a   Juliano, Luiz ^a  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Fluorescent peptide; Fluorogenic substrate; Proteinase; Thiol protease

Indexed keywords

AMINO ACIDS; BIOASSAY; FLUORESCENCE; HYDROLYSIS; QUENCHING;

HYDROPHOBIC SUBSITES;

BIOCHEMISTRY;

2,4 DINITROPHENOL; 3 (2,4 DINITROPHENOL)(2,3 DIAMINOPROPIONIC ACID); AMINO ACID; ANTHRANILIC ACID; ARGININE; AROMATIC AMINO ACID; CARBOXYPEPTIDASE; CATHEPSIN B; EPSILON AMINO 2,4 DINITROPHENOLLYSINE; FLUORESCENT DYE; GLUTAMINE; GLYCINAMIDE; LYSINE; PEPTIDE; PHENYLALANINE; PROPIONIC ACID DERIVATIVE; PROTEINASE; THIOL PROTEINASE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ACCURACY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; HYDROPHOBICITY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; SEQUENCE ANALYSIS;

CATHEPSIN B; DIPEPTIDASES; FLUORESCENT DYES; HUMANS; HYDROLYSIS; PEPTIDES; SUBSTRATE SPECIFICITY;

EID: 0037113185     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020840     Document Type: Article

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