Analysis of disulphide linkages in bovine k-casein oligomers using two-dimensional electrophoresis

Holland, John W., Deeth, Hilton C. and Alewood, Paul F. (2008) Analysis of disulphide linkages in bovine k-casein oligomers using two-dimensional electrophoresis. Electrophoresis, 29 11: 2402-2410. doi:10.1002/elps.200700840


Author Holland, John W.
Deeth, Hilton C.
Alewood, Paul F.
Title Analysis of disulphide linkages in bovine k-casein oligomers using two-dimensional electrophoresis
Journal name Electrophoresis   Check publisher's open access policy
ISSN 1522-2683
Publication date 2008-01-01
Year available 2008
Sub-type Article (original research)
DOI 10.1002/elps.200700840
Open Access Status
Volume 29
Issue 11
Start page 2402
End page 2410
Total pages 9
Editor El Rassi, Ziad
Place of publication Weinheim Germany
Publisher Wiley-VCH Verlag GmbH & Co KGaA
Language eng
Subject C1
090899 Food Sciences not elsewhere classified
860299 Dairy Products not elsewhere classified
Abstract Disulphide bonds play an important role in protein structure and function. Bovine k-casein (k-csn), an important glycoprotein in milk, contains two cysteines that can form disulphide bonds. On 2-D gels run under nonreducing conditions the k-csn in milk presented a complex pattern of monomers and disulphide-linked oligomers. Trains of spots corresponding to monomers to hexamers were observed as a result of the participation of different glycoforms and phosphoforms in oligomer formation. The dimers and trimers ran as doublets on the gel and analysis of the disulphide-linked peptides released from them after in-gel tryptic digestion showed they were the result of different disulphide linkages. The linkages were confirmed by MSMS. When milks with electrophoretically distinct genetic variants of k-csn were mixed and run on 2-D gels, they retained their distinct patterns indicating that disulphide exchange reactions or disulphide ‘scrambling’ was not occurring during 2-D analysis. The patterns observed represent the native distribution of k-csn in milk at harvest. The role and significance of the disulphide bonding of k-csn are discussed. © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Keyword Biochemical Research Methods
Chemistry, Analytical
Biochemistry & Molecular Biology
Chemistry
BIOCHEMICAL RESEARCH METHODS
CHEMISTRY, ANALYTICAL
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

 
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Created: Fri, 17 Apr 2009, 04:03:57 EST by Emma Cushworth on behalf of Institute for Molecular Bioscience