title: Purification and characterization of a novel tyrosyl-aminopeptidase from human osteoclastomas.
abstract: 1. An aminopeptidase that preferentially releases tyrosine residues from synthetic substrates has been purified from human osteoclastomas. This enzyme also hydrolyses dipeptides having an N-terminal tyrosine and a hydrophobic carboxy-terminal amino acid. 2. The tyrosyl-aminopeptidase consists of two identical subunits with M(r)s of about 100,000. 3. The enzyme is a metallopeptidase and is inhibited by chelating agents, chloromethylketone analogues of hydrophobic amino acids, and bestatin.
authors.affiliation: Department of Histopathology, St George's Hospital Medical School, London, U.K.
authors.forename: A E
authors.initials: AE
authors.lastname: Page
authors.forename: M J
authors.initials: MJ
authors.lastname: Warburton
mesh_terms: D000626:Aminopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D001859:Bone Neoplasms / Q000201:enzymology*; D018212:Giant Cell Tumor of Bone / Q000201:enzymology*; D006801:Humans; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D000626:Aminopeptidases; C086415:tyrosyl aminopeptidase