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  • Title: Partial purification of ethanolaminephosphotransferase from rat brain microsomes.
    Author: Vecchini A, Roberti R, Freysz L, Binaglia L.
    Journal: Biochim Biophys Acta; 1987 Mar 13; 918(1):40-7. PubMed ID: 3030437.
    Abstract:
    Rat brain ethanolaminephosphotransferase (CDPethanolamine : 1,2-diacylglycerol ethanolaminephosphotransferase, EC 2.7.8.1) was solubilized by treating rat brain microsomes with buffered solutions containing octyl glucoside or Triton X-100. The solubilized enzyme was stable both at 4 degrees C and at -18 degrees C. A partial purification was obtained using an ion-exchange chromatographic procedure. The partially purified enzyme showed four major bands in SDS-polyacrylamide gel electrophoresis; its specific activity was increased by a factor of 37 compared to that of the membrane-bound enzyme. Glycerol and diacylglycerol were effective as stabilizers. Phosphatidylcholine, lysophosphatidylcholine and phosphatidylserine increased both the specific activity and the stability of the partially purified enzyme.
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