Journal
INTERNATIONAL DAIRY JOURNAL
Volume 13, Issue 1, Pages 15-27Publisher
ELSEVIER SCI LTD
DOI: 10.1016/S0958-6946(02)00127-9
Keywords
bovine alpha(S2)-casein; trypsin; mass spectrometry; peptide kinetics
Categories
Ask authors/readers for more resources
Bovine alpha(S2)-casein was purified by anionic exchange and hydrophobic interaction chromatographies. The purified alpha(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 alpha(S2)-casein in solution was proposed. (C) 2003 Elsevier Science Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available