Moulin A, Giordani R, Teissère M, Piéroni G
Centre de Biochimie et de Biologie moléculaire, C.N.R.S., Marseille.
C R Acad Sci III. 1992;314(8):337-42.
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.
使用一种新方法对来自大戟乳胶的脂肪酶进行了纯化，该方法包括用非极性溶剂萃取以及在硅胶上进行吸附色谱法。脂肪酶（比活性为1500 IU/mg蛋白质）从与脂质复合的硅胶上洗脱下来。主要蛋白质组分的分子量为38000，当与脂质组分分离时无活性。必须使脂质和蛋白质组分重新结合，才能恢复72%的脂解活性。
