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Use of proteomic methodology for the characterization of human milk fat globular membrane proteins

Charlwood, Joanne and Hanrahan, Sarah and Tyldesley, Richard and Langridge, James and 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 0003-2697

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Official URL: http://dx.doi.org/10.1006/abio.2001.5498

Abstract

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: α-lactalbumin, lysozyme precursor, β-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.

Item Type:Article
Additional Information:Online ISSN 1096-0309
Research Community:University of Westminster > Life Sciences, School of
ID Code:4410
Deposited On:17 Jul 2007
Last Modified:15 Dec 2009 10:45

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