title: Tight-binding inhibition of cathepsin S by cystatins.
abstract: Human cystatins A, B and C were purified, and their inhibition efficiency was tested with the cysteine proteinase cathepsin S. Cathepsin S was strongly inhibited by cystatins A and B in the subnanomolar range and by cystatin C in the picomolar range. Two steps of inhibition of cathepsin S by the cystatins which involve slow binding are discussed.
authors.affiliation: Institute of Biochemistry, Faculty of Medicine, Martin-Luther University, Halle (Saale), Germany.
authors.forename: D
authors.initials: D
authors.lastname: Brömme
authors.forename: R
authors.initials: R
authors.lastname: Rinne
authors.forename: H
authors.initials: H
authors.lastname: Kirschke
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002403:Cathepsins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D055313:Cystatin B; D055316:Cystatin C; D015891:Cystatins / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides; D013379:Substrate Specificity
chemical_list: C525030:CST3 protein, human; C524994:CSTB protein, human; D055316:Cystatin C; D015891:Cystatins; D009842:Oligopeptides; D055313:Cystatin B; D002403:Cathepsins; C028217:cathepsin S