Abstract
The cytosol of brain tissue from mature BDF1 mice contains very little dihydrofolate reductase activity but it does contain a high molecular weight nonfunctional protein which cross-reacts in a radioimmunoassay for the active enzyme. Liver cytosal contains less of this high molecular weight cross-reacting protein and more of the functional dihydrofolate reductase. The cytosol from kidney contains very little of the high molecular weight cross-reacting protein, 95% of the immunoreactive proteins being the functional form of dihydrofolate reductase. The modification of dihydrofolate reductase into a nonfunctional form may be an intrinsic property of some cells and this finding could explain the variability in measuring the activity of this enzyme in brain tissue of mature animals.
| Original language | English (UK) |
|---|---|
| Pages (from-to) | 258-262 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 141 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 26 Nov 1986 |
| Externally published | Yes |