Plant lectin proteins have a wide range of biological importance. In this research work the isolation,partial purification and characterization of the lectin proteins from the Soybean seeds (Glycine max) have been reported. The lectin proteins was purified with the help of ion exchange chromatography and further gel filtration chromatography on DEAE Cellulose column and Sephadex G-100 column respectively. Human blood group A was used for the agglutination assay. Lectin Protein concentration was determined by Lowry method and further analysis was done by SDS- PAGE. Samples were dialysed against phosphate buffer saline (PBS) and SDS-PAGE was done to identify the molecular weight of fractions. Further, haemagglutination assay was performed for sample of crude, 20% cut, 60% cut, 90% cut, dialysed samples, 60% ion exchange chromatography portion using A type blood group. The highest titer value was obtained from agglutination assay the sample from gel filtration chromatography i.e.512HU and the specific activity is 6400 HU/mg. The partially purified lectin protein gave a single protein peak on ion exchange chromatography. On SDS-PAGE electrophoretogram, many bands were observed, out of which one band was of 30 kDa which is supposed to be the band of lectin. The partially purified lectin show cytotoxic activity against HeLa cell line. The highest inhibition of HeLa cells i.e. 63.8% was observed at the concentration of 250μg/ml. Thus, the IC50 of partially purified lectin protein was found to be 99.2μl/ml.