Corn Agmatine Iminohydrolase: PURIFICATION AND PROPERTIES.
Corn Agmatine Iminohydrolase: PURIFICATION AND PROPERTIES.
复制标题
玉米胍丁胺亚氨基水解酶：纯化和特性。
作者：
H. Yanagisawa;Y. Suzuki
通过在二乙氨乙基纤维素、Sephadex G-100 和胍丁胺亲和柱上进行色谱分离，将玉米芽提取物中的胍丁胺亚氨基水解酶 (EC 3.5.3.12) 纯化 7,300 倍。根据分析凝胶电泳的标准，该酶是均质的。 Bio-Gel P-200 估计的分子量为 85,000，该酶似乎是具有相同亚基的二聚体（分子量为 43,000）。通过凝胶电聚焦测定的等电点为4.7。活性的最佳pH和温度分别为6.5和60℃。活化能为每摩尔10.9卡。胍丁胺具有高度特异性，其K(m)值为1.9×10(-4)摩尔，并且该酶存在于细胞质中。该酶对Cu(2+)和Zn(2+)敏感，也被对羟基汞苯甲酸酯和arcain抑制。
Agmatine iminohydrolase (EC 3.5.3.12) was purified 7,300-fold from extracts of corn shoots by chromatographic separations on diethylaminoethyl-cellulose, Sephadex G-100, and agmatine-affinity column. The enzyme was homogeneous by the criteria of analytical gel electrophoresis. Molecular weight estimated by Bio-Gel P-200 was 85,000, and the enzyme seems to be a dimer with identical subunits (molecular weight, 43,000). The isoelectric point determined by gel electrofocusing was 4.7. The optimal pH and temperature for activity were 6.5 and 60 C, respectively. The activation energy was 10.9 kilocalories per mole. High specificity exists for agmatine, the K(m) value for agmatine was 1.9 x 10(-4) molar, and the enzyme was present in the cytosol. The enzyme was sensitive to Cu(2+) and Zn(2+) and also was inhibited by p-hydroxymercuribenzoate and arcain.