title: [Purification of lipase from latex of Euphorbia characias by an extraction method with apolar solvent].
abstract: A lipase from the latex of Euphorbia characias was purified using a new method involving extraction by apolar solvent and adsorption chromatography on silica. The lipase (specific activity 1,500 IU/mg of protein) was eluted from silica complexed with a lipid. The main proteic fraction, showing a molecular weight of 38,000, was inactive when dissociated from the lipid fraction. It was necessary to reassociate the lipid and proteic fractions for 72% of the lipolytic activity to be recovered.
authors.affiliation: Centre de Biochimie et de Biologie moléculaire, C.N.R.S., Marseille.
authors.forename: A
authors.initials: A
authors.lastname: Moulin
authors.forename: R
authors.initials: R
authors.lastname: Giordani
authors.forename: M
authors.initials: M
authors.lastname: Teissère
authors.forename: G
authors.initials: G
authors.lastname: Piéroni
mesh_terms: D002855:Chromatography, Thin Layer / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D007840:Latex / Q000737:chemistry*; D008049:Lipase / Q000302:isolation & purification*; D010936:Plant Extracts / Q000032:analysis; D012997:Solvents
chemical_list: D007840:Latex; D010936:Plant Extracts; D012997:Solvents; D008049:Lipase
vernacular_title: Purification d'une lipase dans le latex d'Euphorbia characias par une méthode d'extraction en solvant apolaire.