title: Isolation of two forms of carboxylester lipase (cholesterol esterase) from porcine pancreas.
abstract: Carboxylester lipase (cholesterol esterase, EC 3.1.1.13) has been purified to homogeneity from porcine pancreas. The enzyme is isolated in two molecular mass forms, a monomer of 74 kDa and a dimer of 167 kDa. The dimer consists of two catalytically-active subunits which have molecular masses approximately 9 kDa greater than the monomers. The difference in size was not attributable to carbohydrate or lipid content. The catalytic properties of the two forms are comparable on a weight basis, the amino acid compositions are quite similar, and the N-terminal sequences are nearly identical for 24 residues. These similarities suggest a possible precursor-product relationship between the two carboxylester lipase forms.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000032:analysis; D007527:Isoenzymes / Q000302:isolation & purification*; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D002787:Sterol Esterase / Q000302:isolation & purification*; D013379:Substrate Specificity; D013552:Swine
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D005227:Fatty Acids; D007527:Isoenzymes; D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase