concanavalin-a and blepharismone

PHA, Con-A, or anti-tubulin antibodies inhibit homotypic pair formation, in B, intermedium mating type-I cells in the presence of suboptimal concentrations of gamone II. The inhibition is dependent on the dose of gamone added; the structural conformation and the relative concentration of the inhibitor; and the time of addition of the inhibitor. The block can be selectively prevented by competitive inhibitors of each ligand. The receptors for the inhibitors are distinctive and there is no cross-reaction between the ligands. It is concluded that ligand binding and subsequent receptor-ligand aggregation must induce a change within the cell-surface membrane, which distorts the distribution and/or affects an optimal conformational aspect of a specific membrane-receptor system for the gamon, a prerequisite for cell pair formation.

Topics: Acetylgalactosamine; Aminophenols; Animals; Antibodies; Binding Sites; Cell Membrane; Ciliophora; Concanavalin A; Ferritins; Hydroxybenzoates; Lactates; Lectins; Methylglucosides; Receptors, Drug; Reproduction; Serum Albumin, Bovine; Structure-Activity Relationship; Tubulin