Interaction of lanthanum chloride with human erythrocyte membrane in relation to acetylcholinesterase activity.

Lanthanum chloride (1 mM) inhibits the activity of acetylcholinesterase in vitro in the human erythrocyte membrane. Lineweaver-Burk analysis indicates that lanthanum chloride induced inhibition of acetylcholinesterase activity is competitive in nature. The Arrhenius plot shows that the transition temperature of erythrocyte membrane-bound acetylcholinesterase is significantly reduced in the presence of lanthanum chloride. These results suggest that lanthanum chloride increases the fluidity of the erythrocyte membrane and this may be a cause of inhibition of membrane-bound acetylcholinesterase activity.