Scavenging of Hydrogen Peroxide in the Endosperm of Ricinus communis by Ascorbate Peroxidase

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概要

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• The fat-storing endosperm of Ricinus communis L. was found to contain an ascorbate peroxidase (EC 1.11.1.11), which is nearly as active as catalase (EC 1.11.1.6) in degradation of hydrogen peroxide (H_2O_2) at its physiological concentrations. This ascorbate peroxidase probably functions together with monodehydroascorbate reductase (EC 1.6.5.4) or dehydroascorbate reductase (EC 1.8.5.1) and glutathione reductase (EC 1.6.4.2) to remove the H_2O_2 produced during the transformation of fat to carbohydrate in the glyoxysomes. The activities of these enzymes as well as the content of ascorbate and glutathione increase parallel to the activities of glyoxysomal marker enzymes during the course of germination. Inhibition of catalase by aminotriazole results in increases of the ascorbate peroxidase activity and of the glutathione content. All four enzymes are predominantly localized in the cytosol of the Ricinus endosperm with low activities found in the plastids and the mitochondria. The results suggest, that the ascorbate-dependent H_2O_2 scavenging pathway, which has been shown to be responsible for the reduction of photosynthetically derived H_2O_2 in the chloroplasts, operates also in the Ricinus endosperm.

• 日本植物生理学会の論文

著者

• Zimmer Ina

  Botanical Institute University Of Cologne

• Klapheck Sigrid

  Botanical Institute, University of Cologne

• Cosse Heinz

  Botanical Institute, University of Cologne

• Cosse Heinz

  Botanical Institute University Of Cologne

• Klapheck Sigrid

  Botanical Institute University Of Cologne

関連論文

• Scavenging of Hydrogen Peroxide in the Endosperm of Ricinus communis by Ascorbate Peroxidase
• The Function of Homoglutathione and Hydroxymethylglutathione for the Scavenging of Hydrogen Peroxied

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