Detection of choline kinase in purified rat brain myelin

Tatsuhide Kunishita, Kuldeep K. Vaswani, Charles R. Morrow, Robert W. Ledeen

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)351-355
Number of pages5
JournalNeurochemical Research
Issue number4
StatePublished - Apr 1987

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cellular and Molecular Neuroscience


  • Choline kinase
  • lipid-synthesizing enzyme
  • myelin
  • phosphocholine

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