title: Purification and properties of a lipase from Cephaloleia presignis (Coleoptera, chrysomelidae).
abstract: A novel lipase from the insect Cephaloleia presignis was purified by a procedure involving ammonium sulphate precipitation, and Phenyl Toyopearl 650M, DEAE-5PW and hydrophobic-interaction column chromatographies. The purified lipase was homogeneous with a molecular mass of 31000 Da by SDS/PAGE and of 29000 Da by gel filtration on a Superose 12 column. The enzyme was identified as a glycoprotein with a pI of 6.9. The enzyme unspecifically liberated short-chain to long-chain fatty acids from p-nitrophenyl esters, methyl esters and triglycerides. The N-terminal 28 amino acid residues were determined as AGTLGYATRHVLPIFTLDDYTGSNEMWG, which showed no similarity with known proteins, suggesting that the purified lipase may belong to a novel class of hydrolases.
authors.affiliation: Instituto de Química, UNAM, Circuito Exterior, Ciudad Universitaria, Coyoacán 04510 México, D.F.
authors.forename: R
authors.initials: R
authors.lastname: Arreguín-Espinosa
authors.forename: B
authors.initials: B
authors.lastname: Arreguín
authors.forename: C
authors.initials: C
authors.lastname: González
mesh_terms: D000118:Acetylglucosaminidase / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D001517:Coleoptera / Q000201:enzymology*; D004492:Edetic Acid / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D004791:Enzyme Inhibitors; D008670:Metals; D004492:Edetic Acid; D008049:Lipase; D000118:Acetylglucosaminidase