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. 1981 Apr;67(4):697–700. doi: 10.1104/pp.67.4.697

Corn Agmatine Iminohydrolase

PURIFICATION AND PROPERTIES 1

Hiroshi Yanagisawa 1, Yonezo Suzuki 1
PMCID: PMC425756  PMID: 16661738

Abstract

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 Km value for agmatine was 1.9 × 10−4 molar, and the enzyme was present in the cytosol. The enzyme was sensitive to Cu2+ and Zn2+ and also was inhibited by p-hydroxymercuribenzoate and arcain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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