The roles of fucosylated glycoproteins and oligosaccharides in hepatoma cells were studied by means of fucosylation analysis. It was noted that the protein bands between 23 ku and 40 ku which bound to ulex europaeus agglutinin (UEA) and lens culinaris agglutinin (LCA) reduced significantly until 20 weeks when the liver mass formed, but the band at 80 ku became denser week after week during the course of rat hepatocarcinogenesis induced by N-nitrosodiethylamine. In comparison to the hepatoma cells with low metastatic potential, high metastatic hepatoma cells were found more protein bands binding to UEA and LCA within a broad range of molecular mass. Fucosyltransferase activities were furthermore investigated in the metastatic tissues of hepatoma. It was observed that the activity of 1,6 fucosyltransferase in metastatic liver mass was significantly higher than those of liver tissues without metastasis. Therefore, the fucosylated glycoproteins were isolated and directly used for the treatment of 7721-k3 hepatoma cells. Interestingly the glycoprotein isolated by aleuria aurantia lectin (AAL) and LCA chromatography significantly inhibited the migration of 7721-k3 hepatoma cells. Glycopeptides digested from the glycoproteins above still have the same inhibitory effects on 7721-k3 cells or even stronger. Results by a series of lectin binding analysis showed that these oligosaccharides had a strong affinity to concanavalin A and bound to L-type and E-type phaseolus vulgaris agglutinin as well. This evidence suggested that the fucosylated oligosaccharides might change into high mannose type in hepatocarcinogenesis and played an important role in hepatoma cell migration and metastasis.