Membrane Bound Diacylglycerol Lipases in Bovine Brain: Purification and Characterization

  • Akhlaq A. Farooqui
  • W. Allen Taylor
  • Lloyd A. Horrocks
Part of the FIDIA Research Series book series (FIDIA, volume 4)


It is becoming increasingly evident that diacylglycerols, a minor component of mammalian plasma membranes, regulate the activity of protein kinase C (Berridge, 1984). This enzyme has been implicated in the control of cell division, membrane fusion, differentiation, and signal transduction across the cell membrane (Downes, 1983; Nishizuka 1983, 1984; Das and Rand, 1984; Majerus et al., 1984). Furthermore, diacylglycerols have been reported to stimulate the activities of phospholipases by perturbing the bilayer structure of biological membranes (Dawson et al., 1983; 1984; Watson et al., 1984). In brain, diacylglycerols are either phosphorylated to phosphatidic acid by diacylglycerol kinase (Sun, 1983; Bazan, 1983) or hydrolyzed to free fatty acids and monoacylglycerol by diacylglycerol lipase (Cabot and Gatt, 1976, 1977, 1978; Rousseau et al., 1983; Rousseau and Gatt, 1984; Farooqui et al., 1985a,b).


Bovine Brain Sodium Taurocholate Left Ordinate Monoacylglycerol Lipase Diacylglycerol Lipase 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • Akhlaq A. Farooqui
    • 1
  • W. Allen Taylor
    • 1
  • Lloyd A. Horrocks
    • 1
  1. 1.Department of Physiological ChemistryThe Ohio State UniversityColumbusUSA

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