title: Purification and characterization of tripeptide aminopeptidase from bovine dental follicles.
abstract: Tripeptide aminopeptidase (EC 3.4.11.4) was purified from bovine dental follicles by a series of chromatographies. Purified enzyme had a specific activity of 59.5 units per mg protein with L-prolyl-glycylglycine as substrate. The pH optimum was 8.0. The purified native enzyme had a Mr of 230,000 and was shown to be a tetramer of subunit Mr of 58,000. The isoelectric point was pH 7.0. The enzyme was inhibited by 5-5'-dithio-bis (2-nitrobenzoic acid), o-phenanthroline, and bestatin. Substrate specificity studies indicated that the enzyme specifically hydrolyzes the N-terminal amino acid residue from tripeptides only.
authors.affiliation: Department of Oral Biochemistry, Matsumoto Dental College, Shiojiri-Nagano, Japan.
authors.forename: B Y
authors.initials: BY
authors.lastname: Hiraoka
authors.forename: M
authors.initials: M
authors.lastname: Harada
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D000818:Animals; D002417:Cattle; D003795:Dental Sac / Q000201:enzymology*; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D007202:Indicators and Reagents; D008969:Molecular Sequence Data; D013379:Substrate Specificity
chemical_list: D007202:Indicators and Reagents; D000626:Aminopeptidases; C026045:tripeptide aminopeptidase; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases