PURIFICATION AND CHARACTERIZATION OF LECTIN FROM BAUHINIA CHAMPIONII BENTH.
龙须藤凝集素的分离纯化和性质

Bauhinia championii lectin (BCL) was purified from the seeds of Bauhinia championii Benth. by affinity chromatography on an acid-treated Sepharose 6B column. Hemagglutinating activity of the purified BCL increased by 57 times and the activity recovery was 63.3%. The molecular weight of BCL is 64000 consisting of two identical subunits. The subunit molecular weight is 32000 with isoelectric point of 4.70. BCL is a glycoprotein containing 3.0% of sugar. N-acetyl-D-galactosamine was determined to be a most potent inhibitor of BCL in agglutinating rabbit erythocytes.