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Corn Agmatine Iminohydrolase: PURIFICATION AND PROPERTIES
1Department of Biology, Faculty of Science, Osaka City University, Sumiyoshi-ku, Osaka 558, Japan.
Plant Physiology
|April 1, 1981
Summary
Agmatine iminohydrolase, an enzyme from corn shoots, was purified and characterized. This enzyme plays a crucial role in plant metabolism, showing high specificity for agmatine.
Area of Science:
- Biochemistry
- Plant Physiology
Background:
- Agmatine iminohydrolase (EC 3.5.3.12) is an enzyme involved in metabolic pathways.
- Understanding plant enzymes is crucial for agricultural and biochemical research.
Purpose of the Study:
- To purify and characterize agmatine iminohydrolase from corn shoots.
- To determine the enzyme's kinetic and physical properties.
Main Methods:
- Enzyme purification using sequential chromatography (DEAE-cellulose, Sephadex G-100, agmatine-affinity column).
- Characterization using analytical gel electrophoresis, Bio-Gel P-200, and isoelectric focusing.
- Enzyme activity assays at varying pH, temperature, and substrate concentrations.
Main Results:
- Agmatine iminohydrolase was purified 7,300-fold and found to be homogeneous.
- The enzyme has a molecular weight of 85,000 Da, likely a dimer, with an isoelectric point of 4.7.
- Optimal activity was observed at pH 6.5 and 60°C, with a K(m) of 1.9 x 10(-4) M for agmatine. The enzyme is located in the cytosol.
- The enzyme is sensitive to Cu(2+), Zn(2+), p-hydroxymercuribenzoate, and arcain.
Conclusions:
- Corn shoots contain a highly specific cytosolic agmatine iminohydrolase.
- The characterized properties provide a basis for further functional studies in plant metabolism.