In order to establish and analyze core-fucosylated glycoprotein profiles of human normal liver tissues, which could contribute to the finding of more aberrantly fucosylated glycoproteins related to liver diseases, based on the approach, “lectin affinity chromatography, 2-DE and MALDI-MS/MS”, the lens culinaris agglutinin (LCA) affinity glycoprotein profiles from human normal liver tissues were obtained, in which 130±3 protein spots were detected. Altogether, 90 silver-stained spots in the 2-DE map were cut out, destained and subjected to in-gel tryptic digestion, and 53 proteins were identified by MALDI-TOF MS/MS. These proteins, mainly in the middle range (pI 5～9, M 10～100 ku), were found to participate in the metabolism and play crucial roles in binding and catalytic reactions. Putative N-linked glycosylation consensus sequence, i.e., -N-X-S/T-, was applied to evaluate glycosylation of all the identified proteins. Furthermore, protein immunoprecipitation combined with lectin blot was used to further validate fucosylation of the identified possible candidate proteins, haptoglobin and alpha enolase. All the results suggested that lectin affinity chromatography and 2-DE in combination with MALDI-MS/MS enabled the identification of all the specific subsets of glycoprotein, and the database could give us a help when searching for some aberrantly core-fucosylated glycoproteins associated with some diseases.