Detection of choline kinase in purified rat brain myelin.
Choline kinase, an enzyme involved in the Kennedy pathway conversion of diacylglycerol to phosphatidylcholine, was detected in highly purified rat brain myelin at a level equal to 20% that of whole brain homogenate. This was an order of magnitude higher than the specific activity of lactate dehydrogenase, marker for cytosol. Choline kinase was also detected in the P1, P2, P3, and cytosolic fractions with highest relative specific activity in the latter. Myelin washed with buffered sodium chloride or taurocholate retained most of its kinase, indicating that adsorption of the soluble enzyme was unlikely. The results of mixing experiments and repeated purification further indicated that the enzyme is intrinsic to myelin. This finding in concert with previous studies supports the concept that myelin has all the enzymes needed to convert diacylglycerol to phosphatidylcholine.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002458:Cell Fractionation; D002797:Choline Kinase / Q000378:metabolism*; D008297:Male; D009186:Myelin Sheath / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012965:Sodium Chloride / Q000494:pharmacology; D013347:Subcellular Fractions / Q000201:enzymology; D013656:Taurocholic Acid / Q000494:pharmacology
D012965:Sodium Chloride; D013656:Taurocholic Acid; D009251:NADPH-Ferrihemoprotein Reductase; D010770:Phosphotransferases; D002797:Choline Kinase