Literature DB >> 3298097

Digestion by pancreatic juice of a beta-casomorphin-containing fragment of buffalo beta-casein.

P Petrilli, P Pucci, J P Pelissier, F Addeo.   

Abstract

Degradation by pig pancreatic juice of a beta-casomorphin-containing fragment (tryptic peptide corresponding to residues 49-68 of buffalo beta-casein) was investigated. The FAB/MS (fast atom bombardment mass spectrometry) technique was used to identify the fragments produced by the concerted action of pancreatic proteases. Pancreatic juice, under our experimental conditions, is not able to release beta-casomorphins or morphiceptin from the tryptic peptide sequence. Furthermore, the present report shows that the rapid hydrolysis of a peptide bond by a single protease can prevent the cleavage of peptide bonds by a different protease. Therefore the formation of some peptides in the gastrointestinal tract can depend on the protease ratio.

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Year:  1987        PMID: 3298097     DOI: 10.1111/j.1399-3011.1987.tb02277.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  1 in total

1.  Specific role of endopeptidases in modulating the nature of protein digestion products.

Authors:  L Savoie; R Charbonneau
Journal:  Plant Foods Hum Nutr       Date:  1990-10       Impact factor: 3.921

  1 in total

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