A novel galactose-specific lectin was isolate from the seeds of Glycine wightii. The Glycine wightii lectin (LGw) was purified by affinity chromatography on guar-gum column. Both native and reduced polyacrylamide gel electrophoresis of LGw showed a single proteic band of 45 kDa. The lectin preferentially agglutinated tripsin-treated "A" human erythrocytes, independent of divalent cations (Ca²⁺ and Mn²⁺). The LGw wasn't affected by heating at 30 ^oC for 20 minutes, but lost 80% of the activity when heated 40 ^oC for 5 minutes. Isoelectric focusing in non-dissociating media indicated the presence of a great number of species in the pH range of 6-7. Analysis of near-UV circular dichroism spectrum by Selcon3 method showed that LGw contain a predominance of b-sheet elements. Biological assays indicated that the lectin was able to induce the neutrophil migration in mice. With the aim for investigate the presence of the LGw in callus culture, cotyledon segments of Glycine wightii seeds were inoculated in basal medium MS supplemented with 4.52 mM 2,4-D, 0.46 mM kinetin and sucrose 2 %. The calli obtained after 35 days period were freeze dried, macerated and submitted to extraction of proteins with 100 mM Tris-HCl pH 8.0 buffer containing 150 mM NaCl, for 3 h at room temperature. The presence of the lectin (7 %) in callus culture was detected by Elisa method.