caa a22 4500 465766781 CHVBK 20180323111916.0 cr unu---uuuuu 170327e19901101xx s 000 0 eng 10.1007/BF02544048 doi (NATIONALLICENCE)springer-10.1007/BF02544048 Is intestinal villus phospholipase A2/lysophospholipase bound pancreatic carboxylester lipase? [Elektronische Daten] [N. Mizuno, H. Brockman] Similarities in substrate specificity, localization and molecular weight between villus membrane phospholipase A2/lysophospholipase and carboxylester lipase of pancreatic origin suggested their possible identity. To test this, a preparation of the phospholipase A2/lysophospholipase released from brush border vesicles by papain was compared to authentic, pancreatic carboxylester lipase. Susceptibility of both activities to the inhibitor, diisopropylfluorophosphate, was consistent with their identity, but inconclusive. It also indicated that two populations of phospholipase A2 species may be present in the papain-released preparation. However, comparison of binding of the activities to Sepharose-coupled, anti-carboxylester-lipase IgG indicates that they are immunologically distinct. American Oil Chemists' Society, 1985 Mizuno N. The Hormel Institute, University of Minnesota, 55912, Austin, Minnesota aut Brockman H. The Hormel Institute, University of Minnesota, 55912, Austin, Minnesota aut Lipids Springer-Verlag 25/11(1990-11-01), 760-762 0024-4201 25:11<760 1990 25 11745 https://doi.org/10.1007/BF02544048 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF02544048 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Mizuno N. The Hormel Institute, University of Minnesota, 55912, Austin, Minnesota aut NATIONALLICENCE 700 1- Brockman H. The Hormel Institute, University of Minnesota, 55912, Austin, Minnesota aut NATIONALLICENCE 773 0- Lipids Springer-Verlag 25/11(1990-11-01), 760-762 0024-4201 25:11<760 1990 25 11745 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer