![]() Interestingly, the mass spectrometry analysis of the main band appearing on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) revealed a chloroplast sedoheptulose 1,7-bisphosphatase, a key enzyme of the Calvin cycle, and a chloroplast mRNA-binding protein, suggesting that the DHA reducing capacity could be a side activity or the novel DHAR could be part of a protein complex. It was GSH-dependent and possessed lower affinity to DHA and GSH than the classical DHARs. The novel DHAR was induced after BEA treatment. Kinetic parameters for dehydroascorbate (DHA) and glutathione (GSH) were also determined. DHARs were analyzed in the presence of different electron donors by native and denaturing electrophoresis as well as by western blot and mass spectrometry to identify a novel induced protein with DHAR activity. Tomato plants were treated with 50 µM of BEA the main antioxidant compounds and enzymes were evaluated. They are involved in the plant response to oxidative stress, such as that induced by the mycotoxin beauvericin (BEA). ![]() Dehydroascorbate reductases (DHARs) are important enzymes that reconvert the dehydroascorbic acid (DHA) into ascorbic acid (ASC).
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