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Sidedness of Phosphatidylcholine-Synthesizing Enzymes in Rat Brain Microsomal Vesicles
Authors:Giuseppe Arienti  Lanfranco Corazzi  Louis Freysz  Luciano Binaglia  Rita Roberti  Giuseppe Porcellati
Affiliation:Department of Biochemistry, The Medical School, University of Perugia, Perugia, Italy;Centre de Neurochemie du CNRS and U44 de l'INSERM, Strasbourg, France
Abstract:The sidedness of CDP-choline:1,2-diradylglycerol choline phosphotransferase (EC 2.7.8.2) and of the choline base-exchange activity has been studied in rat brain microsomal vesicles. Proteases (trypsin and pronase) and mercury-dextran have been used as reagents for membrane surface components. All of them could inactivate both enzymes to a good extent, without affecting the morphology or the permeability to sucrose of the vesicles. It is therefore concluded that CDP-choline:1,2-diradylglycerol choline phosphotransferase and the choline base-exchange activity are localized on the outer surface of rat brain microsomal vesicles.
Keywords:Phosphatidylcholine    Phosphocholine transferase    Base-exchange    Brain microsomes    Membrane asymmetry
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