ISOLATION AND PROPERTIES OF A LECTIN FROM THE SEEDS OF BUTEA-MONOSPERMA

A new lectin was purified from the seeds of Butea monosperma by affini ty chromatography on N-acetyl galactosamine-agarose. The purified lect in has an apparent molecular mass of 67000 Da by gel filtration on a S uperose 6HR 10/30 column, The lectin appears to be comprised of two no n-covalently bound subunits with molecular masses of 32000 and 34000 D a, and contains (8%) neutral sugar. The lectin agglutinates human eryt hrocytes but not those of rat, mouse, hamster, goose and pigeon. The a gglutinating activity is inhibited by N-acetyl galactosamine and does not require a divalent ion. It is also stable at up to 80 degrees C fo r 60 min.