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.