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. 1971 Feb;121(4):597–600. doi: 10.1042/bj1210597

Protein-bound phosphorylserine in acid hydrolysates of brain tissue. The determination of [32P]phosphorylserine by ion-exchange chromatography and electrophoresis

D A Jones 1, R Rodnight 1
PMCID: PMC1176634  PMID: 5114971

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 32P-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 [32P]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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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