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Chemical characterization of bioactive peptides from in vivo digests of casein.

Chemical characterization of bioactive peptides from in vivo digests of casein. The in vivo formation of biologically active caseinopeptides was studied. It was proved that bioactive peptides were released in the small intestine of minipigs in the course of luminal digestion of diets containing bovine casein. An opioid peptide and a phosphopeptide were isolated from jejunal chyme and were chemically characterized. The opioid peptide has been identified as a fragment of beta-casein (60-70). This peptide, named beta-casomorphin-11, displayed substantial opioid activity in an opiate receptor-binding assay. The caseinophosphopeptide has been shown to be a fragment of alpha s1-casein (66-74). Casein-derived phosphopeptides exhibit a potent ability to form soluble complexes with Ca and trace elements. Evidence exists that casomorphins and caseinophosphopeptides participate in the regulation of nutrient entry. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of dairy research Pubmed

Chemical characterization of bioactive peptides from in vivo digests of casein.

The Journal of dairy research , Volume 56 (3): -333 – Sep 12, 1989

Chemical characterization of bioactive peptides from in vivo digests of casein.


Abstract

The in vivo formation of biologically active caseinopeptides was studied. It was proved that bioactive peptides were released in the small intestine of minipigs in the course of luminal digestion of diets containing bovine casein. An opioid peptide and a phosphopeptide were isolated from jejunal chyme and were chemically characterized. The opioid peptide has been identified as a fragment of beta-casein (60-70). This peptide, named beta-casomorphin-11, displayed substantial opioid activity in an opiate receptor-binding assay. The caseinophosphopeptide has been shown to be a fragment of alpha s1-casein (66-74). Casein-derived phosphopeptides exhibit a potent ability to form soluble complexes with Ca and trace elements. Evidence exists that casomorphins and caseinophosphopeptides participate in the regulation of nutrient entry.

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ISSN
0022-0299
DOI
10.1017/s0022029900028788
pmid
2760300

Abstract

The in vivo formation of biologically active caseinopeptides was studied. It was proved that bioactive peptides were released in the small intestine of minipigs in the course of luminal digestion of diets containing bovine casein. An opioid peptide and a phosphopeptide were isolated from jejunal chyme and were chemically characterized. The opioid peptide has been identified as a fragment of beta-casein (60-70). This peptide, named beta-casomorphin-11, displayed substantial opioid activity in an opiate receptor-binding assay. The caseinophosphopeptide has been shown to be a fragment of alpha s1-casein (66-74). Casein-derived phosphopeptides exhibit a potent ability to form soluble complexes with Ca and trace elements. Evidence exists that casomorphins and caseinophosphopeptides participate in the regulation of nutrient entry.

Journal

The Journal of dairy researchPubmed

Published: Sep 12, 1989

There are no references for this article.