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pubmed-article:15560483pubmed:dateCreated2004-11-24lld:pubmed
pubmed-article:15560483pubmed:abstractTextThis study investigated the digestion of the milk protein beta-casein with pepsin under gastro-analogous conditions. Peptide sequences were identified using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with post-source decay as well as liquid chromatography-tandem mass spectrometry by means of database searching. The new software tool, Mascot Distiller, improved the identification rate remarkably. In the case of small peptides, such as di- and tri-peptides, which are promising candidates for intestinal absorption and possible biological effects, identification was possible only after spectrum simulation and manual matching. A list of 41 identified peptides having 2-36 amino acids is given, and unexpected cleavage sites for pepsin are reported. Sequence coverage was 75%.lld:pubmed
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pubmed-article:15560483pubmed:authorpubmed-author:RaithKlausKlld:pubmed
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pubmed-article:15560483pubmed:dateRevised2009-1-15lld:pubmed
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pubmed-article:15560483pubmed:year2004lld:pubmed
pubmed-article:15560483pubmed:articleTitleMass spectrometric characterization of peptides derived by peptic cleavage of bovine beta-casein.lld:pubmed
pubmed-article:15560483pubmed:affiliationInstitute of Pharmaceutics and Biopharmaceutics, Martin Luther University Halle-Wittenberg, Wolfgang-Langenbeck-Strasse 4, 06120 Halle (Saale), Germany.lld:pubmed
pubmed-article:15560483pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15560483pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed