Protein-bound phosphorylserine in acid hydrolysates of brain tissue. The determination of [32P]phosphorylserine by ion-exchange chromatography and electrophoresis |
| |
| Authors: | D. A. Jones and R. Rodnight |
| |
| Affiliation: | Department of Biochemistry, Institute of Psychiatry (British Postgraduate Medical Federation, University of London), De Crespigny Park, London S.E.5, U.K. |
| |
| Abstract: | ![]()
1. Partial acid hydrolysates of proteins derived from cortical slices of guinea-pig brain were divided into two parts and fractionated by ion-exchange chromatography and high-voltage electrophoresis. 2. The apparent yield of protein-bound phosphorylserine by the ion-exchange method was about three times that obtained by electrophoresis. 3. The specific radioactivity of phosphorylserine isolated from (32)P-labelled slices by electrophoresis was twice that isolated by chromatography. 4. The discrepancies were found to be due to the presence of unlabelled phosphates of unknown composition in the ;phosphorylserine' fraction obtained by the ion-exchange method. 5. Electrical stimulation of slices respiring in the presence of [(32)P]phosphate increased the specific radioactivity of the total phosphate in the chromatographic ;phosphorylserine' fraction by 53+/-11%, as compared with only 19+/-5% for the phosphorylserine isolated by electrophoresis. |
| |
| Keywords: | |
|
|
