N-acetylserine in horse muscle  acylphosphatase.
A ninhydrin-negative peptide fraction obtained from tryptic digest of carboxymethyl acylphosphatase was isolated by chromatography on a column of PA 28 Beckman resin and analysed for the amino acid composition. Degradation with carboxypeptidase B and A indicated that the sequence of this peptide was: X-Thr-Ala-Arg. The amino-terminal residue was identified as N-acetylserine by high voltage electrophoresis. It is therefore suggested that the sequence of the NH2-terminal portion of CM-acylphosphatase is N-acetyl-Ser-Thr-Ala-Arg. Digestion with carboxypeptidase A and B indicated also that the COOH-terminal portion of CM-acylphosphatase is-Arg-Tyr-OH.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002268:Carboxypeptidases / Q000494:pharmacology; D002855:Chromatography, Thin Layer; D006736:Horses / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D012694:Serine / Q000031:analogs & derivatives* / Q000032:analysis; D014357:Trypsin / Q000494:pharmacology
D000596:Amino Acids; D012694:Serine; D010744:Phosphoric Monoester Hydrolases; D002268:Carboxypeptidases; D014357:Trypsin