Charlwood, Joanne, Hanrahan, Sarah, Tyldesley, Richard, Langridge, James, Dwek, Miriam and Camilleri, Patrick (2002) Use of proteomic methodology for the characterization of human milk fat globular membrane proteins. Analytical Biochemistry, 301 (2). pp. 314-324. ISSN 0003-2697Full text not available from this repository.
Characterization of the major human milk fat globular membrane proteins was carried out using proteomic techniques comprising two-dimensional polyacrylamide gel electrophoresis, followed by in situ PNGase F and trypsin digestion. Matrix-assisted laser desorption/ionization quadropole time-of-flight and electrospray ionization mass spectrometry identified seven major protein components: ?-lactalbumin, lysozyme precursor, ?-casein, clusterin, lactotransferrin, polymeric immunoglobulin receptor precursor, and human milk fat globule EGF-factor 8 protein. Sequence information on the protein-associated glycans was determined by matrix-assisted laser desorption-ionization quadropole time-of-flight hybrid mass spectrometry. This glycan analysis revealed interesting fucosylation branching patterns which may be influential in maternal protection of the newborn against bacterial and viral pathogenic attack.
|Additional Information:||Online ISSN 1096-0309|
|Subjects:||University of Westminster > Science and Technology > Life Sciences, School of (No longer in use)|
|Depositing User:||Miss Nina Watts|
|Date Deposited:||17 Jul 2007|
|Last Modified:||15 Dec 2009 10:45|
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