Blée E, Schuber F
Institut de Biologie Moléculaire des Plantes (CNRS UPR-406), Département d'Enzymologie Cellulaire et Moléculaire, Strasbourg, France.
Biochem J. 1992 Mar 15;282 ( Pt 3)(Pt 3):711-4. doi: 10.1042/bj2820711.
Epoxide hydrolases catalysing the hydration of cis-9,10-epoxystearate into threo-9,10-dihydroxystearate have been detected in soybean (Glycine max) seedlings. The major activity was found in the cytosol, a minor fraction being strongly associated with microsomes. The soluble enzyme, which was purified to apparent homogeneity by (NH4)2SO4 fractionation, hydrophobic, DEAE- and gel-filtration chromatographies, has a molecular mass of 64 kDa and a pI of 5.4.
在大豆(Glycine max)幼苗中已检测到催化顺式-9,10-环氧硬脂酸水合生成苏式-9,10-二羟基硬脂酸的环氧水解酶。主要活性存在于细胞溶质中,一小部分与微粒体紧密相关。通过硫酸铵分级沉淀、疏水色谱、DEAE色谱和凝胶过滤色谱纯化至表观均一的可溶性酶,分子量为64 kDa,pI为5.4。