PURIFICATION AND CHARACTERIZATION OF LECTIN FROM LATHYRUS-SATIVUS

Lectin has been isolated and purified from Lathyrus sativus using ammo nium sulphate precipitation followed by affinity chromatography. The m olecular weight as determined by HPLC was found to be 42kD. The lectin is a tetramer, consisting of two types of subunits of which the heavi er subunit consists of 2 polypeptides of mol wt of about 21 kD and 16 kD while the smaller subunits consists of two polypeptides of about 5k D as. revealed by SDS-PAGE. The most potent sugar inhibitor of the Lat hyrus lectin was found to be alpha-methyl D-mannoside. The N-terminal amino add sequence was similar to that of pea lectin sequence.