The amino acid sequence around the reactive serine in calf-intestinal alkaline phosphatase

Abstract

The dipeptides Asp-SER³²P and Ser³²P-Ala have been isolated from an acid hydrolysate of calf-intestinal alkaline phosphate (orthophosphoric monoester phosphohydrolase, EC 3.I.3.I), which had been ³²P-labelled on a serine residue at the active site, as described earlier. This shows that the amino acid sequence aroun the active serine is ASP-Ser³²P-Ala. The peptides were identified by using an acid hydrolysate of crytalline ovalbumin the same unballed peptides as reference substances.