Use of proteomic methodology for the characterization of human milk fat globular membrane proteins |
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Authors: | Charlwood Joanne Hanrahan Sarah Tyldesley Richard Langridge James Dwek Miriam Camilleri Patrick |
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Institution: | New Frontiers Science Park, GlaxoSmithKline, Third Avenue, Harlow, Essex, CM19 5AW, United Kingdom. |
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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 quadrupole time-of-flight and electrospray ionization mass spectrometry identified seven major protein components: alpha-lactalbumin, lysozyme precursor, beta-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 quadrupole 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. |
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Keywords: | 3-(acetylamino)-6-aminoacridine matrix-assisted laser desorption-ionization quadropole time-of-flight hybrid mass spectrometry N-linked glycosylation proteomics |
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