Is intestinal villus phospholipase A2/lysophospholipase bound pancreatic carboxylester lipase?
- 1 November 1990
- Vol. 25 (11) , 760-762
- https://doi.org/10.1007/bf02544048
Abstract
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.This publication has 20 references indexed in Scilit:
- Molecular cloning and expression of cDNA for rat pancreatic cholesterol esteraseBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1989
- Identity of a cytosolic neutral cholesterol esterase in rat liver with the bile salt stimulated cholesterol esterase in pancreasBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1989
- Solubilization and assay of phospholipase A2 activity from rat jejunal brush-border membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1988
- Regulation of carboxyl ester lipase adsorption to surfaces. 1. Chemical specificityBiochemistry, 1987
- Isolation of purified brush-border membranes from rat jejunum containing a Ca2+-independent phospholipase A2 activityBiochimica et Biophysica Acta (BBA) - Biomembranes, 1987
- Isolation of two forms of carboxylester lipase (cholesterol esterase) from porcine pancreasBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1987
- Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloningBiochemistry, 1987
- Acylenzyme mechanism and solvent isotope effects for cholesterol esterase-catalyzed hydrolysis of p-nitrophenyl butyrateBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1985
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976