Appearance of high-molecular-weight acetylcholinesterase in aneural muscle developing in vivo.
Acetylcholinesterase was studied in the superior oblique muscle of the duck embryo during the course of in vivo development. Normally developing, paralyzed, and uninnervated muscles were studied using velocity sedimentation for separation of various forms and biochemical determination of enzyme activity, and light and electron microscopy for histochemical and cytochemical localization of enzyme. Results indicate that neither muscle activity nor contact by the motor neurons is essential for the appearance of high-molecular-weight form of acetylcholinesterase on muscle cells developing in vivo. Acetylcholinesterase activity per muscle was considerably lower in the paralyzed and aneural muscles than the normal muscle. The absolute loss of acetylcholinesterase parallels loss of muscle protein in paralyzed and aneural muscles and may be secondary. Paralysis or absence of innervation had no significant effect on the specific activity of acetylcholinesterase.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D003472:Curare / Q000494:pharmacology; D004372:Ducks; D008970:Molecular Weight; D009045:Motor Endplate / Q000648:ultrastructure; D009132:Muscles / Q000196:embryology* / Q000294:innervation; D009469:Neuromuscular Junction / Q000201:enzymology
D003472:Curare; D000110:Acetylcholinesterase