Monoamine oxidase activity in hepatopancreas of Octopus vulgaris |
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| Institution: | 1. MOE Key Laboratory of Marine Genetics and Breeding, College of Marine Life Sciences, Ocean University of China, 5 Yushan Road, Qingdao 266003, China;2. Key Laboratory of Tropical Aquatic Germplasm of Hainan Province, Sanya Oceanographic Institution, Ocean University of China, Sanya 572000, China |
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| Abstract: | 1. Monoamine oxidase activity has been studied in hepatopancreas of Octopus vulgaris using 5-HT and PEA as substrates.2. Time courses of MAO activity against 5-HT and PEA show that the enzyme has higher affinity for PEA than for 5-HT.3. MAO activity against 5-HT appears more sensitive than MAO activity against PEA, to variations of the temperature (range 17–67°C).4. The inhibition curves obtained with clorgyline and deprenyl indicate that MAO activity is due to a single form of the enzyme, not corresponding to type A and type B MAO.5. Semicarbazide 10?4 M does not affect the deamination of 5-HT and PEA, demonstrating that a semicarbazide-sensitive amine oxidase is not involved in this process. |
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