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

Authors
Type
Published Article
Journal
The Biochemical journal
Publication Date
Volume
121
Issue
4
Pages
597–600
Identifiers
PMID: 5114971
Source
Medline

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.

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