Schistosoma mansoni: surface membrane isolation by polycationic beads.
The Schistosoma mansoni surface membrane complex was isolated by binding polycationic beads to the worm surface in a sucrose- or sorbitol-acetate buffer, pH 5.0, at 4 C. The ratio of incorporation [3H]cholesterol/[14C]arachidonic acid was measured as well as the specific activities of the alkaline phosphatase (EC 3.1.3.1), Type I phosphodiesterase (EC 3.1.4.1), and Ca2+-adenosine triphosphatase (EC 3.6.1.3). The results indicated that membranes isolated on beads were of comparable or greater purity than membranes isolated by sucrose gradient centrifugation. The isolation procedure was rapid (30 min) and produced membrane fractions whose cytoplasmic surfaces were probably exposed.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002412:Cations; D002458:Cell Fractionation / Q000379:methods*; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure*; D005260:Female; D008297:Male; D008855:Microscopy, Electron, Scanning; D008863:Microspheres; D043264:Phosphodiesterase I; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D012550:Schistosoma mansoni / Q000648:ultrastructure*
D002412:Cations; D000469:Alkaline Phosphatase; D010727:Phosphoric Diester Hydrolases; D043264:Phosphodiesterase I; D000252:Calcium-Transporting ATPases