The ultrastructural localization of acetylcholinesterase activity in the scolex of the cysticercus of Hydatigera taeniaeformis.
Acetylcholinesterase activity in the scolex of the cysticercus of Hydatigera taeniaeformis was studied by means of electron microscopy. Acetylthiocholine iodide was used as the substrate and 10(-4) M of eserine used to inhibit acetylcholinesterase activity. The sites of activity were visualized within the microtriches of the distal cytoplasm, muscle bundles, cytoplasm, vesiculated bodies, flame cells and hooks of the rostellar region. Enzyme activity was also localized within the nuclear membrane, neuroplasm, and membranes of nerve cells.
D000110:Acetylcholinesterase / Q000032:analysis*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002467:Cell Nucleus / Q000201:enzymology; D002589:Cestoda / Q000201:enzymology* / Q000648:ultrastructure; D002923:Cilia / Q000201:enzymology; D003552:Cysticercus / Q000201:enzymology; D009132:Muscles / Q000201:enzymology; D009474:Neurons / Q000201:enzymology / Q000648:ultrastructure
D000110:Acetylcholinesterase