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Tryptic hydrolysis of bovineαS2-casein: identification and release kinetics of peptides

Authors
Journal
International Dairy Journal
0958-6946
Publisher
Elsevier
Publication Date
Volume
13
Issue
1
Identifiers
DOI: 10.1016/s0958-6946(02)00127-9
Keywords
  • BovineαS2-Casein
  • Trypsin
  • Mass Spectrometry
  • Peptide Kinetics
Disciplines
  • Biology

Abstract

Abstract Bovine α S2-casein was purified by anionic exchange and hydrophobic interaction chromatographies. The purified α S2-casein was hydrolysed with trypsin; the resulting peptides were identified by amino acids composition and on line reversed-phase high performance liquid chromatography coupled with electrospray mass spectrometry. A study on the kinetics of peptide release enabled discrimination between different protein areas according to their surface-accessibility. Data from the kinetic study were reconciled with secondary structure predictions and a hypothetical model of the structural organisation of purified bovine α S2-casein in solution was proposed.

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