A novel and efficient method for purification of soybean agglutinin (SBA) from soybean was reported. The method was characterized by selective extraction of SBA from soybean homogenate with barbiturate buffer (pH 6 2), removal of impurity by hydroxyapatite, and the final purification of SBA by guaran affinity chromatography. The purified SBA showed a single band of 27 5 kD by SDS PAGE. The lowest concentration of SBA that caused agglutination of the rabbit red blood cells was 0 31 mg/L. Agglutination of different cancer cell lines by the purified SBA was examined. Strong agglutination of the human nasopharyngeal CNE cells, mouse Lewis lung carcinoma cells, and rat mammary adenocarcinoma R3230AC cells was observed. However, SBA could not agglutinate the human hepatocellular carcinoma BEL 7402 cells, suggesting that unlike the above mentioned three cell lines, the BEL 7402 cells may not express N acetylgalactosamine (GalNAc) or galactose (Gal) residues in significant amount at the non reducing terminals of their cell surface glycans.
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