Low-abundance proteome of chicken egg white were studied by using combinatorial peptide ligand libraries(CPLL) and the linear ion trap quadrupole(LTQ) mass spectrometry.The effect of salt concentration and elution order on the enrichment efficiency of CPLL was investigated.The results showed that the higher salt concentration，the stronger interaction between the egg white protein solutions，which effected CPLL enrichment efficiency significantly.The lysozyme could be separated effectively in the order of urea CHAPS(3-［3-cholamidopropyldimethylammonio］-1-propansulfonate) elution first ，HOS(hydro-organic solution) the second elution.High effective enrichmental conditions of CPLL were chicken egg white with 150 mmol/L NaCl,25 mmol/L KH2PO4，pH 8.8，urea CHAPS elution.Through the analysis of the SDS-PAGE band difference with 60 μg protein loaded after CPLL enrichment，45 species of low abundance proteins from chicken egg white were identified by LTQ mass spectrometry，of which two species were not reported yet.The result of subcellular localization analysis showed that egg white protein secreted protein was 19 species，which was in the majority.The number of unknown subcellular location of proteins from chicken egg white was taken the second placeThis paper shows that the CPLL technology is rapid，simple and sensitive，and is suitable for the determination and confirmation of the low-abundance protein in chicken egg white，that the depth of which reach the sub cellular level.