Abstract
Alkaline phosphatase (E. C. 3. 1. 3. 1) from human kidney was purified by n-butanol extraction, ammonium sulfate fractionation, and chromatography over DEAE-cellulose, CM-cellulose, and Sephadex G-200. The purified enzyme exhibited a single protein band by disc electrophoresis. This enzyme was activated by MgCl2 and NiCl2, but inhibited by CdCl2, and had an optimum pH at 11.4. Other properties of kidney alkaline phosphatase were also investigated and discussed.
