Kinetic studies of catechol-o-methyltransferase from the brain of the African catfish,Clarias gariepinus |
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| Institution: | 1. Università degli studi di Roma “Tor Vergata”, Italy;2. Università degli Studi della Campania “Luigi Vanvitelli”, Italy;3. Università degli Studi di Napoli “Parthenope”, Italy;1. State Key Laboratory of Atmospheric Boundary Layer Physics and Atmospheric Chemistry, Institute of Atmospheric Physics, Chinese Academy of Sciences, Beijing 100029, PR China;2. Key Laboratory for Yellow River and Huai River Water Environment and Pollution Control, Ministry of Education, School of Environment, Henan Normal University, Xinxiang 453007, PR China;3. Key Laboratory of Mountain Surface Processes and Ecological Regulation, Institute of Mountain Hazards and Environment, Chinese Academy of Sciences, Chengdu 610041, PR China;4. Institute for Meteorology and Climate Research, Atmospheric Environmental Research, Karlsruhe Institute of Technology, Garmisch-Partenkirchen D-82467, Germany;5. Pioneer Center Land-CRAFT, Department of Agroecology, Aarhus University, Aarhus C, 8000, Denmark |
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| Abstract: | - 1.1. Optimum in vitro conditions, and kinetics of the enzyme catechol-O-methyltransferase from the brain of the male African catfish were studied.
- 2.2. A saturated level for S-adenosylmethionine, as methyldonor, and magnesium as cofactor was reached at 5 μM and 10 mM, respectively.
- 3.3. The addition of ascorbic acid, as an antioxidant, and tranylcypromine, as a MAO inhibitor, was not necessary, during incubations with fore-brain homogenates.
- 4.4. Kinetic analysis of the methylation of catecholestrone, catecholestradiol and dopamine showed Km values of 1.2, 0.6 and 0.5 μM, respectively.
- 5.5. The affinity of the catecholsubstrates for the enzyme catechol-O-methyltransferase is much higher in the brain of the African catfish than in tissues of mammals.
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