An active site peptide from human placental alkaline phosphatase.
A preparation of human placental alkaline phosphatase was labelled covalently at the active site with [32P]orthophosphate. Treatment with trypsin gave essentially one radioactive peptide, the active site peptide, of approximately 2300 molecular weight. Dansylation of the peptide showed that the amino-terminal residue was glycine. After acid hydrolysis the only radioactively-labelled amino acid present was serine phosphate. The amino acid composition was similar to those compositions reported for active site peptides from other alkaline phosphatases.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D005260:Female; D006801:Humans; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification*; D010710:Phosphates / Q000378:metabolism; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D010710:Phosphates; D000469:Alkaline Phosphatase; D014357:Trypsin