Abstract
A new lectin was purified from the seeds of Butea monosperma by affinity chromatography on N-acetyl galactosamine-agarose. The purified lectin has an apparent molecular mass of 67 000 Da by gel filtration on a Superose 6HR 10/30 column. The lectin appears to be comprised of two non-covalently bound subunits with molecular masses of 32 000 and 34 000 Da, and contains (8%) neutral sugar. The lectin agglutinates human erythrocytes but not those of rat, mouse, hamster, goose and pigeon. The agglutinating activity is inhibited by N-acetyl galactosamine and does not require a divalent ion. It is also stable at up to 80°C for 60 min.
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