ausblenden:
Schlagwörter:
PEPTIDE LIGAND LIBRARIES; EGGSHELL MEMBRANE-PROTEINS; MASS-SPECTROMETRY;
EMBRYONIC-DEVELOPMENT; LIQUID-CHROMATOGRAPHY; GEL-ELECTROPHORESIS;
VITELLINE MEMBRANE; CALCIFIED LAYER; MATRIX PROTEIN; ORGANIC MATRIXBiotechnology & Applied Microbiology; Food Science & Technology;
Microbiology;
2D-electrophoresis; Egg white allergens; Eggshell; Oviduct; Yolk
Zusammenfassung:
Before the application of mass spectrometry–based proteomics to egg white, a mere 15 chicken egg white proteins were identified and characterized by at least partial amino acid sequences. After the publication of the chicken genome sequence and derived protein sequence databases in 2004, various proteomic surveys increased this number to 167 proteins that were identified by at least two sequence-unique peptides. Since then many comparative proteomic papers have been published describing changes in the egg white proteome upon storage at different temperatures over different time spans, changes associated with early embryonic development, differences between egg varieties, and proteome modifications induced by stress. Egg white proteins do not occur exclusively in egg white. Proteomic analysis detected major egg white proteins, such as ovalbumin and ovotransferrin, in all other compartments of the egg, including the shell. An interesting application of egg white proteomics is the analysis of food for the presence of potentially harmful egg white allergens.
