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Plant and Cell Physiology, 1985, Vol. 26, No. 5 787-795
© 1985

Article

Characteristics of a Urate-Degrading Diamine Oxidase-Peroxidase Enzyme System in Soybean Radicles

Shigeyuki Tajima1, Takeshi Kanazawa2, Eiko Takeuchi3 and Yukio Yamamoto4

1 Department of Agricultural Chemistry, Kagawa University Miki-cho, Kita-gun, Kagawa 761-07, Japan
2 Otsuka Assay Laboratories, Otsuka Pharmaceutical Co., Ltd. Kawauchi-cho, Tokushima 771-01, Japan
3 Yamasei Co. Ltd. Ayagami-cho, Ayauta-gun, Kagawa 761-07, Japan
4 School of Agriculture, Nagoya University Chikusa-ku, Nagoya 464, Japan

The cadaverine content of soybean radicles showed a maximum peak 3–4 days after planting. The variation coincided with radicle uricase activity during seed germination.

The uricase activity could not be fractionate when the buffer pH for the extraction was at 6.0. The addition of 1 M KCl or NaCl to the buffer allowed the extraction of the uricase activity, but an addition of 1 M MgCl2 or BaCl2 inhibited this enzyme's activity.

The urate-degrading enzyme system was purified 248-fold per milligram of protein from soybean radicles. The respective Km values of the diamine oxidase activity for cadaverine and of the urate-degrading activity for hydrogen peroxide and urate were 1.25, 2.93 and 50.3 µM. Analysis by gel electrophoresis of the partially purified enzyme fraction revealed that the urate-degrading enzyme system consisted of a peroxidase that degrades urate with hydrogen peroxide and a diamine oxidase that releases hydrogen peroxide.

These data are evidence that a urate-degrading diamine oxidase and peroxidase system exists in soybean radicles and that the reaction rate of urate-degradation is controlled by the concentration of cadaverine.

(Received November 28, 1984; Accepted April 8, 1985)
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