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.


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  (ERA 2012 Listed)    (ERA 2010 Rank A)   Check publisher's open access policy
Publication date 2008
Sub-type Article
DOI 10.1002/elps.200700840
Volume number 29
Issue number 11
ISSN 1522-2683
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
Collection year 2009
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
Q-Index Code C1
Q-Index Status Confirmed Code

 
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Created: Thu, 16 Apr 2009, 18:03:57 EST by Emma Cushworth on behalf of Institute for Molecular Bioscience