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

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. I...

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2002-10, Vol.23 (10), p.1773-1781
Main Authors: Fosset, S, Fromentin, G, Gietzen, D.W, Dubarry, M, Huneau, J.F, Antoine, J.M, Lang, V, Mathieu-Casseron, F, Tomé, D
Format: Article
Language:English
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Summary: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 μg/ml at 60 min.
ISSN:0196-9781
1873-5169
DOI:10.1016/S0196-9781(02)00134-1