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Purification and characterization of a novel tyrosyl-aminopeptidase from human osteoclastomas
1Department of Histopathology, St George's Hospital Medical School, London, U.K.
The International Journal of Biochemistry
|January 1, 1994
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.