Hemagglutinin(HA)is a type Ⅰ transmembrane glycoprotein which is located in the surface of the influenza virus envelope. It plays a pivotal role in binding with sialyloligosaccharides receptor on host cell surface and mediated viral entry into cells. It is also the important target of neutralizing antibodies and vaccine development. The glycosylation of HA is closely associated with viral virulence, host range and other infections. In addition, glycosylation and pattern alterations also affect the structural roles as well as diverse functional roles of HA in many specific biological process. However, little is known about the precise glycan structures on the surface of HA. In this study, we prepared a specific SAα2-3Gal Magnetic Particle Conjugates, which was used to purify HA from avian influenza A (H7N2) virus. The isolated HA was identified by SDS-PAGE and MALDI-TOF-MS. Then, the glycan profile of HA was analyzed by the lectin microarrays and mass spectrometry. The results showed that the glycan structures such as fucose, galactose, N-acetylgalactosamine, mannose, and N-acetylglucosamine were expressed on the surface of HA and 16 glycans with the precise structure were acquired. These glycans may be associated with the biological functions of HA, and helps to reveal the glycan mechanism of avian influenza virus how to effect the host specificity, virulence and infectivity of the influenza virus, as well as design the vaccine based on glycan structures on the surface of HA.