A group of serine peptidases, the prolyl oligopeptidase family, cannot hydrolyze peptides
containing more than about 30 residues. This group is unrelated to the classical trypsin and …

Prolyl oligopeptidase (POP) is a serine peptidase which digests small peptide-like
hormones, neuroactive peptides, and various cellular factors. Therefore, this peptidase has …

Macrophages are immune cells crucial for host defense and homeostasis maintenance, and
their dysregulation is involved in multiple pathological conditions, such as liver fibrosis. The …

Prolyl endopeptidase (PE), a protease that cleaves after proline residues in oligopeptides, is
highly active in brain and degrades neuropeptides in vitro. We have recently demonstrated …

Prolyl endopeptidase is a protheolytic enzyme which could have a neuropeptide
catabolising role in the central nervous system. Although prolyl endopeptidase has been …

Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing
peptides shorter than 30 amino acids. POP may be associated with cognitive functions …

Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing
peptides shorter than 30-mer, including many bioactive peptides. The distribution of POP in …

Prolyl oligopeptidase (PO, EC 3.4. 21.26) is a post-proline cleaving enzyme with
endopeptidase activity towards peptides not longer than 30 amino acids. It has been purified …

BACKGROUND AND PURPOSE A serine protease, prolyl oligopeptidase (POP) has been
reported to be involved in the release of the pro‐angiogenic tetrapeptide acetyl‐N‐Ser‐Asp …

Trypanosoma brucei contains a soluble serine oligopeptidase (OP-Tb) that is released into
the host bloodstream during infection, where it has been postulated to participate in the …