Isolation of two forms of carboxylester lipase (cholesterol esterase) from porcine pancreas.
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.
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
D000596:Amino Acids; D002241:Carbohydrates; D005227:Fatty Acids; D007527:Isoenzymes; D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase