A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure

Biochemistry. 1986 Dec 2;25(24):8089-94. doi: 10.1021/bi00372a044.

Abstract

A new acylphosphatase from human erythrocytes was isolated by an original purification procedure. It is an isoenzyme of the well-characterized human skeletal muscle acylphosphatase. The erythrocyte enzyme shows hydrolytic activity on acyl phosphates with higher affinity than the muscle enzyme for some substrates and phosphorylated inhibitors. The sequence was determined by characterizing the peptides purified from tryptic, peptic, and Staphylococcus aureus V8 protease digests of the protein, and it was found to differ in 44% of the total positions as compared to the human muscle enzyme. About one-third of these differences are in the form of strictly conservative replacements. The protein consists of 98 amino acid residues; it has an acetylated NH2-terminus and does not contain cysteine: (sequence in text).

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Anhydride Hydrolases*
  • Amino Acid Sequence
  • Erythrocytes / enzymology*
  • Humans
  • Isoenzymes / blood*
  • Isoenzymes / isolation & purification
  • Kinetics
  • Mass Spectrometry
  • Muscles / enzymology
  • Peptide Fragments
  • Phosphoric Monoester Hydrolases / blood*
  • Phosphoric Monoester Hydrolases / isolation & purification

Substances

  • Isoenzymes
  • Peptide Fragments
  • Phosphoric Monoester Hydrolases
  • Acid Anhydride Hydrolases
  • acylphosphatase