title: Isolation and partial characterization of the tegumental outer membrane of adult Schistosoma mansoni.
abstract: Incubation of adult Schistosoma mansoni at 37 degrees C in chemically defined media caused the shedding of variable amounts of the parasite's tegument. In phosphate-buffered saline, pH 7.4, 37% of 125I-labelled wheat germ agglutinin which was attached to the schistosome surface was released within 5 min. When the released material was collected by centrifugation at 55 000 g for 1 h, the pellet was seen to consist of components of the parasite tegument and contained 1% of the parasite protein and 6.2% of the 5'-AMPase activity. By monitoring the release of the gut enzyme, haemoglobinase, it was shown that predominantly tegumental material was released under these conditions. The material released from the parasite was separated by discontinuous sucrose gradient centrifugation into 4 major fractions and it was shown that a material banding at low density was highly enriched in vesicles of parasite outer membrane. Major polypeptides of apparent molecular weights 135 000, 110 000, 90 000, 65 000, 47 000 and 40 000 and glycoproteins of apparent molecular weights 135 000, 120 000, 65 000, 63 000 and 30-40 000 were identified in this fraction. Comparison of the distribution of 5'-AMPase activity and the contents of each fraction as revealed by ultrastructural examination showed that this enzyme is a good marker for the tegumental outer membrane.
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000032:analysis / Q000201:enzymology / Q000648:ultrastructure; D002499:Centrifugation, Density Gradient; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D009708:Nucleotidases / Q000378:metabolism; D012550:Schistosoma mansoni / Q000032:analysis / Q000648:ultrastructure*
chemical_list: D008565:Membrane Proteins; D009708:Nucleotidases; C018775:adenosine monophosphatase