Protein-bound phosphorylthreonine in some tissues and organisms

摘要: Abstract 1. The amounts of protein-bound [32P]phosphorylthreonine in some tissues and organisms were determined after labelling with [32P]orthophosphate expressed relation to the [32P]phosphorylserine isolated. Baker's yeast, rat liver, muscle, human erythrocytes Escherichia coli displayed a ratio 1:8, 1:21, 1:23, 1:38, respectively. 2. When baker's yeast was incubated for different periods time 32P-labelling phosphorylthreonine parallelled that phosphorylserine. This suggests main part two labelled phosphoamino acids derived from same or related proteins. 3. Assuming specific radioactivity acids, total calculated ratios above previously reported liver representing nucleated cells, found contain 70, 20, 20 nmoles per g, respectively, E. coli, cells without nuclei, less than 2 nmoles/g.