Triosephosphate isomerases in Italian ryegrass ( Lolium multiflorum ): characterization and susceptibility to herbicides.
Daniele Del Buono, Bhakti Prinsi, Luca Espen, Luciano Scarponi
Index: J. Agric. Food Chem. 57(17) , 7924-30, (2009)
Full Text: HTML
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-time-dependent 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.
Related Compounds
Related Articles:
2007-04-01
[Appl. Environ. Microbiol. 73(8) , 2697-707, (2007)]
Forced evolution of a herbicide detoxifying glutathione transferase.
2003-06-27
[J. Biol. Chem. 278(26) , 23930-5, (2003)]
Taxonomic distribution of plant glutathione S-transferases acting on xenobiotics.
2000-06-01
[Phytochemistry 54(3) , 267-73, (2000)]
2009-01-23
[J. Mol. Biol. 385(3) , 984-1002, (2009)]
2011-11-23
[J. Agric. Food Chem. 59(22) , 12109-15, (2011)]