Distribution of brush-border membrane peptidases along the rat intestine

Pharm Res. 1994 Jun;11(6):897-900. doi: 10.1023/a:1018946228432.


The longitudinal distribution of brush-border endopeptidase-24.11, endopeptidase-2, aminopeptidase W, angiotensin-converting enzyme (ACE), dipeptidyl peptidase IV (DPP IV), carboxypeptidase P, and aminopeptidase P in the rat intestine was determined. The jejunum has the highest activities of endopeptidase-24.11 and ACE while the ileum has the highest activities of aminopeptidase W and carboxypeptidase P, and the jejunoileal junction has the highest activity of aminopeptidase P. The jejunum and ileum have similar activities of DPP IV. The profiles of differential hydrolysis of neurotensin and acetylneurotensin (8-13) along the intestine agree with distribution of endopeptidase-24.11 and ACE, suggesting that amino acid sequences of peptides and the substrate specificity of enzymes will determine site-dependent hydrolysis. There is substantial similarity in the intestinal distribution of peptidases in the human, rat, and rabbit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Ileum / enzymology
  • In Vitro Techniques
  • Intestinal Mucosa / enzymology*
  • Intestinal Mucosa / ultrastructure
  • Jejunum / enzymology
  • Male
  • Microvilli / enzymology
  • Molecular Sequence Data
  • Organ Specificity
  • Peptide Hydrolases / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Spectrophotometry, Ultraviolet


  • Peptide Hydrolases