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EN
Acetylcholinesterase (AChE) sequentially extracted from mature specimens of Hymenolepis diminuta was shown to be a globular protein, the monomeric form of which (Ga₁) had molecular mass of 66 kDa as determined by SDS-PAGE. Amphiphilic character of the enzyme was revealed by Triton X-l14 phase partitioning. The cestode AChE preferred acetylthiocholine over propionyl- and butyrylthiocholine as substrate, split N-acetyl-ß-methylthiocholine and myristoylcholine but did not hydrolyze ß-carbonaphthoxycholine, a substrate for butyrylcholinesterases. It was sensitive to 10⁻⁵ M physostigmine and 10⁻⁵ M BW284C51 but not to 10⁻³ M iso-OMPA. No butyrylcholinesterase activity was detected in extracts from the parasite.
EN
The distribution of acetylcholinesterase (AChE) in oncospheres and developing cysticercoids of Hymenolepis diminuta was examined. The enzyme was localized in the nervous system and in some non-nerve cells of these larvae. In oncospheres AChE was detected in hook muscles and in the binucleated medullar center that is known to enclose two neurons. At early developmental stages of the cysticercoids the enzyme was localized in the post-oncospheral hook muscles and in subtegumental muscle fibers of the cercomer. At medium and late stages of development the activity of AChE was detected in the developing nervous system and in two and, subsequently, in four populations of cells, which gradually spread over the whole internal wall of the cyst, thus forming a thin multilayer AChE-positive lining of the cyst cavity. Following withdrawal of the scolex the lining separates the parenchyma of the turned neck from the cyst tissues and remains AChE-positive during the whole life of the parasite, i.e. up to the death of the infected host. The role played by non-neural AChE associated with the cyst cavity lining is unknown, but seems to regulate both the transport of nutrients and minerals into the scolex and waste substances in the opposite direction.
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