Sidedness of Phosphatidylcholine-Synthesizing Enzymes in Rat Brain Microsomal Vesicles |
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Authors: | Giuseppe Arienti Lanfranco Corazzi Louis Freysz Luciano Binaglia Rita Roberti Giuseppe Porcellati |
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Affiliation: | Department of Biochemistry, The Medical School, University of Perugia, Perugia, Italy;Centre de Neurochemie du CNRS and U44 de l'INSERM, Strasbourg, France |
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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. |
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Keywords: | Phosphatidylcholine Phosphocholine transferase Base-exchange Brain microsomes Membrane asymmetry |
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