Premium
The chicken egg white proteome
Author(s) -
Mann Karlheinz
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700397
Subject(s) - egg white , ovalbumin , proteome , biology , protein sequencing , peptide sequence , white (mutation) , biochemistry , amino acid , sequence (biology) , computational biology , microbiology and biotechnology , genetics , gene , antigen
Using 1‐D PAGE and LC‐MS/MS and MS 3 we identified 78 chicken egg white proteins, 54 of which were identified in egg white for the first time. All proteins were quantitated by calculating their exponentially modified protein abundance index (emPAI). Some previously known egg white components not characterized by amino acid sequences before, such as α‐2‐macroglobulin, were associated to a sequence for the first time. The predicted sequence was confirmed by MS‐sequenced peptides covering 42% of the entire sequence. α‐2‐Macroglobulin occurred in egg white at the same concentration as ovostatin with which it showed 35% identity. For other proteins, which were previously only characterized by partial sequences, such as β‐ovomucin or ovalbumin X, we identified and confirmed predicted complete sequences with a high coverage by MS‐sequenced peptides. New proteins included a 7 kDa protein consisting of a single secretoglobin sequence (ovosecretoglobin), a 7 kDa protein with similarity to black swan cygnin and turkey meleagrin (gallin) and proteins involved in binding, modification, and possibly detoxification, of bacterial lipopolysaccaride. The list of egg white proteins provided is by far the most comprehensive at present and is intended to serve as a starting point for the isolation and functional characterization of interesting new proteins.