Use of Proteomic Methodology for the Characterization of Human Milk Fat Globular Membrane Proteins

✍ Scribed by Joanne Charlwood; Sarah Hanrahan; Richard Tyldesley; James Langridge; Miriam Dwek; Patrick Camilleri

• Publisher: Elsevier Science
• Year: 2002
• Tongue: English
• Weight: 241 KB
• Volume: 301
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1006/abio.2001.5498

✦ Synopsis

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 desorptionionization 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.