Ogunyemi E O, Pittner F, Hoffmann-Ostenhof O
Hoppe Seylers Z Physiol Chem. 1978 May;359(5):613-6.
Using the technique of affinity chromatography on NAD-Sepharose the myo-inositol-1-phosphate synthase of Lemna gibba was purified to homogeneity. The molecular and catalytic properties of this enzyme differ very much from those of myo-inositol-1-phosphate synthase from animal sources. Thus the specific activity of the duckweed enzyme is more than two orders of magnitude higher than that of the enzyme from rat testes. It is inhibitied by EDTA and can be reactivated by Mn2. Its molecular weight (135000 +/- 5000), its subunit composition (3 subunits with identical electrophoretic behaviour) and its isoelectric point (pH 7.7) are also very different from the corresponding parameters for the animal enzyme.
利用NAD-琼脂糖亲和层析技术，将浮萍的肌醇-1-磷酸合酶纯化至同质。该酶的分子和催化特性与动物源肌醇-1-磷酸合酶有很大不同。因此，浮萍酶的比活性比大鼠睾丸中的酶高两个多数量级。它受EDTA抑制，可被Mn2+重新激活。其分子量（135000±5000）、亚基组成（3个具有相同电泳行为的亚基）和等电点（pH 7.7）也与动物酶的相应参数有很大差异。
