Isolation and characterization of agglutinin receptor sites: III. Studies on the interaction with other lectins

Abstract

1.1. A wheat germ agglutinin receptor fraction isolated from surface membranes of leukemia cells failed to interact with concanavalin A but did interact to a lesser degree with two other agglutinins.2.2. A preparation of concanavalin A that was not multivalent but presumably monovalent and which blocked the agglutination of susceptible cells by intact concavalin A had no effect on the agglutinability of the same cells by wheat germ agglutinin.3.3. Antiserum against the isolated wheat germ agglutinin receptor fraction from leukemia cells did not react with the normal lymphocytes nor did it react with red blood cells of syngeneic mice.4.4. The same antiserum against the wheat germ agglutinin receptor fraction inhibited the agglutination of L1210 (leukemia), Py 3T3 and Py BHK cells by wheat germ agglutinin but had no effect on the agglutination by concanavalin A of Py 3T3 or Py BHK cells.5.5. It was concluded that at least some lectin receptors are chemically and topographically on the membrane distinct from each other.