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以40%～70%饱和度硫酸铵分级沉淀、DEAESepharoseiCL-6B、SephadexG-100、羟基磷灰石、PhenylSepharoseCL-4B和制备电泳分离纯化了小麦的尿卟啉原合酶(UROS)。酶的亚基分子质量为54ku,全酶分子质量为66ku,酶的等电点6.3,在pH8.2时比活为257μmol/(mg·min),最适反应温度40℃,5mmol/L的巯基乙醇和Mg2+促进酶活,纯化的小麦UROS在-20℃下0.1mol/L,pH8.5的Tris-HCl,内含质量分数为50%的甘油,5mmol/L的巯基乙醇和MgCl2中贮藏7d酶活损失90%。
The uroporphyrinogen synthase (UROS) of wheat was isolated and purified by fractional precipitation of ammonium sulfate with 40% -70% saturation, DEAE Sepharose CL-6B, Sephadex G-100, hydroxyapatite and PhenylSepharose CL-4B. The molecular mass of enzyme subunit was 54ku, the total enzyme molecular weight was 66ku, the isoelectric point of enzyme was 6.3, the specific activity was 257μmol / (mg · min) at pH 8.2, the optimal reaction temperature was 40 ℃, 5mmol / L Mercaptoethanol and Mg2 + to promote enzyme activity. The purified wheat UROS was stored at -20 ℃ 0.1mol / L, pH8.5 Tris-HCl, containing 50% glycerol, 5mmol / L mercaptoethanol and MgCl2 7d 90% loss of activity.