[Erythrocyte membrane in Duchenne muscular dystrophy. III. Modifications of acetylcholinesterase]. / Studi sulle membrane eritrocitarie nella distrofia muscolare tipo Duchenne: III--modificazioni dell' acetilcolinesterasi.

Membrane-bound acetylcholinesterase was assayed in erythrocyte ghosts from patients with Duchenne Muscular Distrophy and from the members of their family. Modifications was observed both in Km and Vmax, indicating changes in conformations of the enzyme.

Fluidity of erythrocyte membranes from patients with Duchenne muscular dystrophy: studies in intact erythrocytes and in ghosts.

We have studied the alterations of fluidity in intact erythrocytes and in erythrocyte membranes from patients with Duchenne muscular dystrophy. The interest of this study was to comparison directly two types of results; these demonstrate an increase of fluidity in the erythrocytic membranes, no changes are present when the label is incorporated in intact erythrocytes. It might be inferred that hypotonic haemolysis removes components that are more weakly bound in Duchenne membranes, and that exert an immobilizing effect on the membrane lipids.

Molecular mechanism of general anesthesia: III. Kinetic studies on erythrocyte ghost acetylcholinesterase.

General anesthetics inhibit erythrocyte membrane-bound acetylcholinesterase. Release of the membrane-bound enzyme by sonication into a soluble form induces a loss of sensitivity to anesthetics. Reconstitution of the solubilized enzyme with phospholipids restores its inhibition by anesthetics. The results suggest that anesthetic inhibition of acetylcholinesterase is mediated through the lipid bilayer.