Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1544, Issue 1-2, 2001, Pages 113-122

  Pimenta, Daniel C ^a   Oliveira, Andreza ^a   Juliano, Maria A ^a   Juliano, Luiz ^a  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Antichymotrypsin; Cathepsin D; Fluorogenic substrate; Kallistatin; Serpin

Indexed keywords

CATHEPSIN D; CYSTATIN C; HYDROLASE; KALLIKREIN; KALLISTATIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; COMPETITIVE INHIBITION; COMPLEX FORMATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SPECIFICITY; HUMAN; MOLECULAR DYNAMICS; PEPTIDE SYNTHESIS; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REACTION ANALYSIS;

AMINO ACID SEQUENCE; CARRIER PROTEINS; CATHEPSIN D; FLUORESCENT DYES; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; LIVER; PEPTIDE FRAGMENTS; SERPINS; SUBSTRATE SPECIFICITY;

EID: 0035846971     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00209-0     Document Type: Article

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