USE OF AN IMMOBILIZED HUMAN ENDOGENOUS LECTIN FOR THE PURIFICATION OF COMPLEMENTARY LIGANDS

1. A galactoside-specific endogenous lectin isolated from human brain was covalently immobilized on divinylsulfone-activated agarose. This highly selective affinity adsorbent proved to be useful in purifying soluble protein ligands. 2. The maximum binding capacity of the adsorbent for complementary proteins was calculated to be 618-mu-g per g of gel (wet resin). 3. Sequential elutions using 0.1M lactose, 0.3M lactose and 0.5M NaCl, and competition assays using incorporation in the presence 0.1M lactose revealed differences in lectin-ligand interactions.