Pub. Date : 1994 Apr
PMID : 7925685
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Bovine lens aldose reductase (ALR2) is readily modified by glutathione disulphide (GSSG) to an enzyme form (GS-ALR2) exhibiting a reduced catalytic efficiency with all the substrates tested and a reduced susceptibility to inhibition. | Glutathione Disulfide | lens aldose reductase pseudogene | Bos taurus |
| 2 | Bovine lens aldose reductase (ALR2) is readily modified by glutathione disulphide (GSSG) to an enzyme form (GS-ALR2) exhibiting a reduced catalytic efficiency with all the substrates tested and a reduced susceptibility to inhibition. | Glutathione Disulfide | lens aldose reductase pseudogene | Bos taurus |
| 3 | By measuring the residual activity of ALR2 incubated in different glutathione redox buffers at 25 degrees C, an apparent redox equilibrium constant of 1.4 +/- 0.1 was evaluated. | Glutathione | lens aldose reductase pseudogene | Bos taurus |
| 4 | Thus the rate and the maximal extent of ALR2 inactivation are proportional to the redox ratio of the thiol used as modifying agent (i.e. [GSH]/[GSSG]). | Sulfhydryl Compounds | lens aldose reductase pseudogene | Bos taurus |
| 5 | Thus the rate and the maximal extent of ALR2 inactivation are proportional to the redox ratio of the thiol used as modifying agent (i.e. [GSH]/[GSSG]). | Glutathione | lens aldose reductase pseudogene | Bos taurus |
| 6 | Thus the rate and the maximal extent of ALR2 inactivation are proportional to the redox ratio of the thiol used as modifying agent (i.e. [GSH]/[GSSG]). | Glutathione Disulfide | lens aldose reductase pseudogene | Bos taurus |
| 7 | A reduced efficiency in the enzyme-cofactor binding following the GSSG dependent modification of ALR2, appears to be associated to the thiol accessibility of GS-ALR2 measured at different temperatures. | Glutathione Disulfide | lens aldose reductase pseudogene | Bos taurus |
| 8 | A reduced efficiency in the enzyme-cofactor binding following the GSSG dependent modification of ALR2, appears to be associated to the thiol accessibility of GS-ALR2 measured at different temperatures. | Sulfhydryl Compounds | lens aldose reductase pseudogene | Bos taurus |
| 9 | Besides being a general feature of protein reactivity in oxidative conditions, the glutathione-mediated ALR2 modification might be part of a cell strategy to preserve reducing power in conditions of oxidative stress. | Glutathione | lens aldose reductase pseudogene | Bos taurus |