| Literature DB >> 109082 |
Abstract
Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa, was purified to homogeneity. The pure enzyme is a glycoprotein containing a very small amount of sugar. It is composed of only one subunit of 50,000 mol. wt. and possesses 1 zinc atom per molecule. Its specificity is primarily directed towards tripeptides with an N-terminal proline residue. However, the enzyme is also able to hydrolyse other tripeptides, except those with either a charged amino acid in the N-terminal position or a proline residue in the second position. The purified aminotripeptidase accounts for almost all the tripeptidase activity of the soluble fraction from intestinal mucosa.Entities:
Mesh:
Substances:
Year: 1979 PMID: 109082 PMCID: PMC1186443 DOI: 10.1042/bj1770801
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857