Purification and characterization of a novel tyrosyl-aminopeptidase from human osteoclastomas.
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.
Page
A E
AE
Department of Histopathology, St George's Hospital Medical School, London, U.K.
Warburton
M J
MJ
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
D000626:Aminopeptidases; C086415:tyrosyl aminopeptidase