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- W2383156066 abstract "Bauhinia championii lectin (BCL) was purified from the seeds of Bauhinia championii Benth. by affinity chromtography 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 64 000 consisting of two identical subunits. The subunit molecular weight is 32 000 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." @default.
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- W2383156066 date "2001-01-01" @default.
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- W2383156066 title "Purification and characterization of lectin from Bauhinia championii Benth." @default.
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