Peptide fragments released from Phe-caseinomacropeptide in vivo in the rat

S. Fosset (1) , G. Fromentin (2) , D. W. Gietzen , M. Dubarry , J. F. Huneau (2) , J. M. Antoine (1) , V. Lang (1) , F. Mathieu-Casseron (1) , Daniel Tomé (2)

1 Danone Research
2 PNCA - Physiologie de la Nutrition et du Comportement Alimentaire

The aim of this study was to investigate the pharmacokinetics of bovine Phe-caseinomacropeptide (Phe-CMP) in the rat after oral administration. This polypeptide was monophosphorylated and mainly nonglycosylated: Phe-CMP-1P. During gastrointestinal digestion and absorption, Phe-CMP-1P was degraded. Intact Phe-CMP-1P and CMP-1P were rapidly released from the stomach. In contrast, partial hydrolysis by pancreatic enzymes was observed. In vitro hydrolysis by brush-border membrane vesicles also indicated that the peptide was degraded. In the blood, "CMP-immunoreactive material" appeared rapidly, reaching a maximum level of 5.5 microg/ml at 60 min.

S. Fosset, G. Fromentin, D. W. Gietzen, M. Dubarry, J. F. Huneau, et al.. Peptide fragments released from Phe-caseinomacropeptide in vivo in the rat. Peptides, 2002. ⟨hal-00294380⟩