HISTOCHEMICAL AND BIOCHEMICAL OBSERVATIONS ON CHOLINESTERASES OF CATS TAPEWORM TAENIA TAENIAFORMIS
HISTOCHEMICAL AND BIOCHEMICAL OBSERVATIONS ON CHOLINESTERASES OF CATS TAPEWORM TAENIA TAENIAFORMIS
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DOI：
10.1111/j.1748-1716.1968.tb04099.x
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发表时间：
1968-01-01
期刊：
影响因子：
--
通讯作者：
TAKKI, S
中科院分区：
文献类型：
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作者：
ERANKO, O;KOUVALAINEN, K;TAKKI, S
用Koelle法对绦虫胆碱酯酶活性进行了组织化学研究，以乙酰硫代胆碱和丁酰硫代胆碱为底物，用瓦尔堡法对绦虫胆碱酯酶活性进行了生物化学研究，以乙酰胆碱、乙酰-[β]-甲基胆碱和丁酰胆碱为底物。抑制剂为乙丝氨酸、四异丙基焦磷酰胺（iso-OMPA）、1，5-双（4-三甲基铵苯基）-3-戊酮二碘（BW 62 C 47）和1，5-双（4-烯丙基甲基铵苯基）-3-戊酮二碘（BW 284 C 51）。无论是组织化学和生物化学证明绦虫胆碱酯酶活性很容易抑制低浓度的艾司氯胺酮，但耐其他抑制剂，无论使用的底物。在这方面，绦虫胆碱酯酶活性明显不同于人血清、大鼠脑匀浆或猫十二指肠中的胆碱酯酶活性，这些物质被用作胆碱酯酶的参考来源。乙酰硫代胆碱和丁酰硫代胆碱，有或没有异OMPA或BW 62 C 47的组织化学胆碱酯酶反应，表现出相同的分布，选择性地限于神经节，神经干和神经纤维的蠕虫，包括那些支配吸盘。它的结论是绦虫胆碱酯酶是不同的哺乳动物乙酰胆碱酯酶和非特异性胆碱酯酶，即使它是，像乙酰胆碱酯酶，选择性神经酶和过量的底物抑制。
Cholinesterase activity of the tapeworm was studied histochemically with the Koelle method, using acetylthiocholine and butyrylthiocholine as substrates, and biochemically with the Warburg technique, using acetylcholine, acetyl-[beta]-methylchollne and butyryl-choline as substrates. Eserine, tetra-isopropylpyrophosphoramide (iso-OMPA), 1,5-bis (4-trlmethylammonlum-phenyl)-pentan-3-one dliodide (BW 62 C 47) and 1,5-bis(4-allylmethyl-ammonlumphenyl)pentan-3-one diiodide (BW 284 C 51) were used as inhibitors. Both the histo-chemlcally and the biochemically demonstrable tapeworm cholinesterase activity was readily inhibited by low concentrations of eserine but resistant to the other inhibitors employed, whatever substrate was used. In this respect the tapeworm cholinesterase activity markedly differed from that in the human serum, the rat brain homogenate or the duodenum of the cat, which were used as reference sources of cholinesterase. The histochemical cholinesterase reactions obtained with acetylthiocholine and butyrylthiocholine, with or without iso-OMPA or BW 62 C 47, showed identical distributions, selectively limited to nervous ganglia, nerve trunks and nerve fibers of the worm, including those innervating the suckers. It is concluded that the tapeworm cholinesterase is distinct from mammalian acetylcholinesterase and non-specific cholinesterase, even if it is, like acetylcholinesterase, a selectively neuronal enzyme and inhibited by excess substrate.