These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification of two lipases with high phospholipase A1 activity from guinea-pig pancreas.
    Author: Fauvel J, Bonnefis MJ, Sarda L, Chap H, Thouvenot JP, Douste-Blazy L.
    Journal: Biochim Biophys Acta; 1981 Feb 23; 663(2):446-56. PubMed ID: 7213780.
    Abstract:
    1. Two cationic lipases (Ia and Ib) were purified from homogenates of fresh guinea-pig pancreas by ion-exchange chromatography on DEAE-Sepharose and CM-Sepharose (twice for the latter) followed by gel filtration on Sephadex G-100. 2. Both enzymes were homogeneous upon polyacrylamide gel electrophoresis. Their molecular weights are 37,000 and 42,000 for lipases Ia and Ib, respectively, as determined by gel filtration on Sephadex G-100. Very close values for isoelectric points were found in the pH range 9.3-9.4. 3. The cationic lipases are characterized by a high phospholipase A activity (500 IU/mg protein using a potentiometric assay with egg yolk lecithin as substrate), resulting in an unusual phospholipase/lipase activity ratio of 1. 4. Using doubly labelled phosphatidylcholine, a specificity, A1, was described for the two enzymes, which are unaffected by N-ethylmaleimide, diisopropylfluorophosphate and p-bromophenacylbromide. The enzymes are insensitive to EDTA and slightly inhibited by CaCl2 and MgCl2, whereas sodium deoxycholate is required for maximal activity.
    [Abstract] [Full Text] [Related] [New Search]