Figures & data
Figure 1. Concentrations of free protein thiols and thiol disulphides (either intramolecular disulphide bridges or thiols, engaged in mixed protein-glutathione disulphides (a) in salt-treated suspension cultures of Dactylis glomerata L. Columns represent mean values ±SD (n = 3). Thiol disulphides-to-free thiols ratio in proteins is represented in part (b).
Figure 2. Diagonal gel electrophoresis for detection of protein thiol disulphides in salt-treated suspension cultures of Dactylis glomerata L. 10% T SDS PAGE were performed in two consecutive dimensions (non-reducing and reducing). Arrows indicates proteins above the diagonal (putative intramolecular disulphide bonds) and proteins below the diagonal (putative glutathionylated proteins). Gels were silver stained.
Figure 3. Thioredoxin/thioredoxin reductase system activity in salt-treated suspension cultures. Columns represent mean values and ±SD (n = 3). Significant values, compared to controls are indicated (*) as calculated by Student's t-test, p < 0.05. Activity is expressed as mmol oxidized NADPH per minute per g protein.
Figure 4. Glutaredoxin activity (a) in salt-treated suspension cultures. Columns represent mean values and ±SD (n = 3). Significant values, compared to controls are indicated (*) as calculated by Student's t-test, p < 0.05. Activity is expressed as mmol oxidized NADPH per minute per g protein. Glutathionylated bovine serum albumin was used as substrate. Glutathionylation of bovine serum albumin was monitored on 10% T SDS PAGE by the shift in the apparent molecular weight (b).
