Properties of Pancreatic Phospholipases A1 and Intestinal Phospholipase A2 from Guinea Pig: Their Complementary Role in the Intestinal Absorption of Phospholipids

  • Ama Diagne
  • Josette Fauvel
  • Salvador Mitjavila
  • Hugues Chap
  • Louis Douste-Blazy
Part of the NATO ASI Series book series (NSSA, volume 116)


In various mammalian species, intestinal absorption of dietary phospholipids requires a previous hydrolysis of the substrate to lysophospholipids and free fatty acids1,2. This is generally achieved by pancreatic phospholipase A2 which is secreted as a trypsin-activable zymogen3. As an exception to other species, we previously reported the absence, in guinea pig pancreas, of classical secretory phospholipase A2 which is replaced by two cationic lipases (Ia and Ib)displaying a high phospholipase Al activity with no evidence for a zymogen form4. These enzymes, which are also found in pancreatic juice, were purified until homogeneity5 and gel filtration on Sephadex G100 of lipases Ia and Ib revealed molecular weights of 37 and 47 Kd respectively. Very close values for isoelectric points were found in the pH range of 9.3–9.4


Intestinal Absorption Pancreatic Juice Brush Border Membrane Sodium Taurocholate Mevalonic Acid 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Ama Diagne
    • 1
  • Josette Fauvel
    • 1
  • Salvador Mitjavila
    • 2
  • Hugues Chap
    • 1
  • Louis Douste-Blazy
    • 1
  1. 1.Hôpital PurpanINSERM Unité 101ToulouseFrance
  2. 2.INSERM Unité 87ToulouseFrance

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