Utilization of membranous lipid substrates by membranous enzymes. Hydrolysis of sphingomyelin in erythrocyte ‘ghosts’ and liposomes by the membranous sphingomyelinase of chicken erythrocyte ‘ghosts’

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Abstract
Incubation at 37.degree. C of hemolyzed chicken erythrocytes (chicken erythrocyte ghosts) resulted in hydrolysis of the membrane sphingomyelin, suggesting an activation of a latent sphingomyelinase during the hemolysis procedure. When this incubation was continued for several hours, the entire sphingomyelin of the erythrocyte ghosts was hydrolyzed and membranes were obtained that were devoid of sphingomyelin but had an active sphingomyelinase. Mixing the latter membranes with human erythrocyte ghosts or positively charged liposomes led to hydrolysis of the sphingomyelin in these 2 membranes. After hemolysis the apparently activated sphingomyelinase in the membrane of the chicken erythrocyte ghosts could apparently hydrolyze sphingomyelin in its own membrane (intramembrane utilization) or adjacent membranes (intermembrane utilization).