The effect of treatments with four herbicides and a safener on the activity of triosephosphate isomerase (TPI) extracted from shoots of Italian ryegrass was investigated. It was found that atrazine and fluorodifen, herbicides which interfere with photosynthesis, caused a decrease in measured enzyme activity. In addition, the in vitro effect of oxidized glutathione (GSSG), a compound produced in situations of oxidative stress, on TPI activity was investigated. It was shown that GSSG was a strong inhibitor of enzyme activity, at low concentrations in a dose-timedependent manner. The enzyme extracts were submitted to chromatographic purifications and to two-dimensional electrophoresis. Some spots had molecular masses ranging between 20 and 30 kDa and were characterized and identified by LC-ESI-MS/MS as TPIs. The mass spectrometry also made it possible to identify the presence of cysteine residues that could be subjected to S-glutathionylation, which regulate the enzyme activity.
Triosephosphate Isomerases in Italian Ryegrass (Lolium multiflorum) : Characterization and Susceptibility to Herbicides / D. Del Buono, B. Prinsi , L. Espen, L. Scarponi. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - 57:17(2009 Aug 06), pp. 7924-7930. [10.1021/jf901681q]
Triosephosphate Isomerases in Italian Ryegrass (Lolium multiflorum) : Characterization and Susceptibility to Herbicides
B. PrinsiSecondo
;L. EspenPenultimo
;
2009
Abstract
The effect of treatments with four herbicides and a safener on the activity of triosephosphate isomerase (TPI) extracted from shoots of Italian ryegrass was investigated. It was found that atrazine and fluorodifen, herbicides which interfere with photosynthesis, caused a decrease in measured enzyme activity. In addition, the in vitro effect of oxidized glutathione (GSSG), a compound produced in situations of oxidative stress, on TPI activity was investigated. It was shown that GSSG was a strong inhibitor of enzyme activity, at low concentrations in a dose-timedependent manner. The enzyme extracts were submitted to chromatographic purifications and to two-dimensional electrophoresis. Some spots had molecular masses ranging between 20 and 30 kDa and were characterized and identified by LC-ESI-MS/MS as TPIs. The mass spectrometry also made it possible to identify the presence of cysteine residues that could be subjected to S-glutathionylation, which regulate the enzyme activity.File | Dimensione | Formato | |
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