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Sidedness of Phosphatidylcholine‐Synthesizing Enzymes in Rat Brain Microsomal Vesicles
Author(s) -
Arienti Giuseppe,
Corazzi Lanfranco,
Freysz Louis,
Binaglia Luciano,
Roberti Rita,
Porcellati Giuseppe
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb07109.x
Subject(s) - vesicle , choline , phosphatidylcholine , biochemistry , phosphotransferase , chemistry , microsome , enzyme , trypsin , membrane , phospholipid
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.