Corn Agmatine Iminohydrolase: PURIFICATION AND PROPERTIES.
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.
Yanagisawa
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Department of Biology, Faculty of Science, Osaka City University, Sumiyoshi-ku, Osaka 558, Japan.
Suzuki
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