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

ABSTRACT

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.