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- W2370652578 abstract "Bauhinia variegata lectin(BVL) has been purified from the seed of Bauhinia variegata L. by affinity c hromatography on an acid-treated Sepharose 6B column . The hemagglutinating act ivity of the purified BVL increased 159 times and the activity recovery is 49.0 %. The molecular weight is 81 000 and the molecule consists of two identical sub units. Its isoelectric point is 4.95. N-acetyl-D-galactosamine is the most p otent inhibitors of BVL. Lactose and galactose can also inhibit the agglutinati on of rabbit erythocytes by BVL." @default.
- W2370652578 created "2016-06-24" @default.
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- W2370652578 date "2000-01-01" @default.
- W2370652578 modified "2023-09-25" @default.
- W2370652578 title "Purification and Characterization of Lectin from Bauhinia variegataL." @default.
- W2370652578 hasPublicationYear "2000" @default.
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