Phosphoesterases of Bacillus subtilis: II. Crystallization and Properties of Alkaline Phosphatase*

Abstract

A procedure for the purification and crystallization of alkaline phosphatase [EC 3.1.3.1] of B. subtilis is described, and several chemical properties of the purified enzyme are reported. The enzyme appears when the cells are grown under the condition of inorganic phosphate deprevation and is probably located in the cell tightly bound to the cell membrane or wall. The enzyme activity is inhibited with EDTA and this inhibition is recovered by the addition of cobalt or zincion. The amino acid composition and amino terminal residue of alkaline phosphatase have been determined.