Hydrolysis of Phosphopeptides. I. Acid Hydrolysis of O-Phosphoryl-DL-serylglycine and Glycyl(O-phosphoryl)-DL-Serine. Sequence Inversion in Dilute Hydrochloric Acid.

Publisher Website
Google Scholar
Abstract
The hydrolysis of SerP-Gly and Gly-SerP in 2 N hydrochloric acid at 100[degree] and in conc. hydrochloric acid at 37[degree] was studied by column chromatographic separation of the hydrolysis products on an anion exchange resin. In 2 N hydrochloric acid sequence inversion occurs with both phosphopeptides. Gly-SerP is hydro-lysed faster than SerP-Gly in both conc. and 2 N acid and hydrolysis takes place almost entirely at the peptide bond. SerP-Gly is largely dephos-phorylated to serylglycine.