The technology of lectin microarrays was established for glycoprotein analysis and initially applied to analyze the glycopattern of whole cell extraction of Chang's liver cells. ConA and GNA were immobilized on the epoxysilane-caoted slides, the standard glycoprotein RNaseB was labeled with Cy3 fluorescent dye, the detection system of lectin microarrays was established for glycoprotein detection and analysis based on the principle of lectin to glycan binding affinity. The consequence of experiment indicated that phosphate buffer containing 1% BSA was the optimal blocking buffer, the optimal incubation time and temperature as well as incubation buffer were 3 hours, room temperature and phosphate buffer containing 1% BSA and 0.05% Tween-20, respectively. Additionally, the specificity of lectin microarrays was validated through the mannose competition assay. Further, the lectin micoarrays containing 10 lectins were fabricated and used to detect and analyze the glycan construction of RNaseB and Fetuin, the result verified the feasibility of our homemade lectin microarray. Eventually they were initially applied to analyze the glycopattern of whole cell extraction of Chang's liver cells. The results indicated that some glycan structure such as multivalent Sia or GlcNAc, terminalα-1,3 mannose, GalNAc and Galβ-1,4GlcNAc possibly existed in the whole cell extraction of Chang's liver cells. Glycosylation is one of the most significant posttranslational modifications of proteins, which plays an indispensable role in a wide variety of biological processes including bacterial infection, cell differentiation, tumor metastasis and cell concretization. Hence, the study on glycosylation draws the attention of researchers widely, but the process develops slowly due to lacking a method can investigate protein-carbohydrate interactions in a rapid, exact and high-throughput manner. The coming lectin microarrays possess the requests above and will promote the process of glycosylation research.