Fluorescent, internally quenched, peptides for exploring the pH-dependent substrate specificity of cathepsin B

Journal of Peptide Science

Volumn 12, Issue 7, 2006, Pages 455-461

  Ruzza, Paolo ^a   Quintieri, Luigi ^b   Osler, Alessio ^a   Calderan, Andrea ^a   Biondi, Barbara ^a   Floreani, Maura ^b   Guiotto, Andrea ^a   Borin, Gianfranco ^a  

^a CNR   (Italy)

^b UNIVERSITY OF PADOVA   (Italy)

Author keywords

Anticancer prodrugs; Cathepsin B; Flouroscence; Internally quenched peptides

Indexed keywords

ALANINE; ALPHA AMINO ACID; ANTINEOPLASTIC AGENT; ARGININE; ASPARTIC ACID; BETA ALANINE; CATHEPSIN B; GLUTAMINE; LYSINE; PEPTIDE DERIVATIVE; PHENYLALANINE; VALINE; ZINC;

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL REACTION KINETICS; ENZYME ASSAY; ENZYME SPECIFICITY; FLUORESCENCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; PEPTIDE SYNTHESIS; PH; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; RESIDUE ANALYSIS;

ANIMALS; CATHEPSIN B; CATTLE; FLUORESCENT DYES; HYDROGEN-ION CONCENTRATION; KINETICS; OLIGOPEPTIDES; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY;

EID: 33745944379     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.748     Document Type: Article

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