Properties of pure acyl phosphatase from bovine brain.

Acyl phosphatase has been purified 25,000-fold from bovine brain. The enzyme is more than 97% pure by acrylamide gel disc electrophoresis. The calculated molecular weight from gel filtration measurements on Sephadex G-75 was 12,100; the value calculated from the amino acid composition was 8,732. Independent determinations of free -SH groups and tyrosine content were in agreement with the amino acid analysis. Lysine is the COOH-terminal amino acid residue. There is no detectable NHz-terminal amino acid residue, suggesting that the a-amino group of the NH2terminal amino acid residue is substituted.