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Plant and Cell Physiology, 1997, Vol. 38, No. 2 173-178
© 1997

Research Paper

Purification and Characterization of Dehydroascorbate Reductase from Rice

Yoshihiro Kato1, Jun'ichi Urano1, Yasushi Maki2 and Takashi Ushimaru1,3

1 Department of Biology, Faculty of Science, Shizuoka University 836 Ohya, Shizuoka, 422 Japan
2 Department of Botany, Faculty of Science, Kyoto University Kyoto, 606-01 Japan

3Corresponding author, e-mail: ushimaru{at}sci.shizuoka.ac.jp

Dehydroascorbate reductase (DHAR; EC 1.8.5.1 [EC] ) is an enzyme that is critical for maintenance of an appropriate level of ascorbate in plant cells. This report describes the purification and characterization of a GSH-dependent DHAR from rice (Oryza saliva) bran and is the first, to our knowledge, of such an analysis of DHAR from a monocot. The enzyme was a monomeric thiol enzyme, resembling DHARs purified from dicots, but it was different from them in terms of heat stability and antigenicity. The amino-terminal amino acid sequence of the DHAR from rice did not show any obvious similarity to those of known proteins with DHAR activity, such as, glutaredoxin (thioltrans-ferase), protein disulfide isomerase, and trypsin inhibitor. Immunoprecipitation analysis showed that this enzyme was a major DHAR in etiolated seedlings. Western blot analysis indicated that this enzyme was distributed ubiquitously in rice tissues. A similar protein was found in barley but not in dicots.

(Received July 18, 1996; Accepted December 4, 1996)
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