Human skeletal muscle acylphosphatase: the primary structure.
Human skeletal muscle acylphosphatase, purified by a technique based on affinity chromatography on immunoadsorbent, has been sequenced completely using tryptic and peptic peptide series, prepared by reverse-phase high-pressure liquid chromatography. The sequence analysis was carried out on all the isolated tryptic peptides using a manual Edman degradation technique and time-course analysis of the released amino acids by carboxypeptidase A. The enzyme is NH2-blocked and the blocking group has been identified by fast atom bombardment mass spectrometry.
D017766:Acid Anhydride Hydrolases; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D006801:Humans; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids; D010446:Peptide Fragments; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase