A. Nicotra et al., MONOAMINE-OXIDASE ACTIVITY IN HEPATOPANCREAS OF OCTOPUS-VULGARIS, Comparative biochemistry and physiology. C. Comparative pharmacologyand toxicology, 106(2), 1993, pp. 479-482
1. Monoamine oxidase activity has been studied in hepatopancreas of Oc
topus vulgaris using 5-HT and PEA as substrates. 2. Time courses of MA
O activity against 5-HT and PEA show that the enzyme has higher affini
ty for PEA than for 5-HT. 3. MAO activity against 5-HT appears more se
nsitive than MAO activity against PEA, to variations of the temperatur
e (range 17-67-degrees-C). 4. The inhibition curves obtained with clor
gyline 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. Semicar
bazide 10(-4) M does not affect the deamination of 5-HT and PEA, demon
strating that a semicarbazide-sensitive amine oxidase is not involved
in this process.