Properties of Pure Acyl Phosphatase from Bovine Brain

This is the authors' abstract. We don't add key points for this paper.

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 NH2-terminal amino acid residue, suggesting that the α-amino group of the NH2-terminal amino acid residue is substituted.