title: Inhibitory activities of partially degraded salivary cystatins.
abstract: 1. Aminoterminally truncated forms of cystatin S and cystatin SN had higher inhibition constants for ficin, but lower ones for cathepsin C (dipeptidyl peptidase I) as compared to their respective full-sized form. 2. Cystatin SN still retained the inhibitory activity for ficin after reduction and carboxymethylation, although the inhibition constant increased.
authors.affiliation: Nippon Dental University Junior College at Niigata, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Isemura
authors.forename: E
authors.initials: E
authors.lastname: Saitoh
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D020789:Cathepsin C; D015891:Cystatins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000037:antagonists & inhibitors; D005361:Ficain / Q000037:antagonists & inhibitors*; D006801:Humans; D007700:Kinetics; D008745:Methylation; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D012469:Salivary Glands / Q000737:chemistry
chemical_list: D015891:Cystatins; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D020789:Cathepsin C; D005361:Ficain