title: Purification of monomeric agmatine iminohydrolase from soybean.
abstract: Agmatine iminohydrolase (EC 3.5.3.12) was purified to homogeneity from the cytosol of soybean (Glycine max) axes by chromatographic separations on Sephadex G-25, Bio-rex 70, and agmatine-affinity columns. The enzyme was homogeneous by the criteria of analytical gel electrophoresis. Molecular weights estimated by Sephadex G-100 gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis were 70,000, indicating that the soybean axes enzyme is a monomer, in contrast to the dimeric enzymes from corn and rice. The isoelectric point determined by gel electrofocusing was 7.5, higher than that of the corn enzyme (4.7). The optimal pH and temperature for activity were 6.5 and 50 degrees C, respectively. The enzyme has high specificity for agmatine, and the Km for agmatine was 2.5 x 10(-3) molar. The enzyme was sensitive to Cu2+ and also was inhibited by p-hydroxymercuribenzoate.
authors.affiliation: Department of Biochemistry, College of Science, Yonsei University, Seoul, Korea.
authors.forename: K H
authors.initials: KH
authors.lastname: Park
authors.forename: Y D
authors.initials: YD
authors.lastname: Cho
mesh_terms: D000376:Agmatine / Q000378:metabolism; D002850:Chromatography, Gel; D003300:Copper / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000302:isolation & purification*; D007231:Infant, Newborn; D007525:Isoelectric Focusing; D007700:Kinetics; D012275:Oryza / Q000201:enzymology*; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity / Q000187:drug effects; D003313:Zea mays / Q000201:enzymology*
chemical_list: D000376:Agmatine; D003300:Copper; D006867:Hydrolases; C019626:agmatine deiminase