1. Alkaline phosphatase from rat liver was separated into tow components by gel filtration. 2. Both components had the same temperature and pH optima, were inhibited by high concentrations of urea and had the same activity towards hydrolysis of phenyl disodium phosphate and p-nitrophenyl phosphate. 3. They differed in electrophoretic mobility, sensitivity to inactivation by heat and digestion by neuraminidase, response to low concentrations of urea, and catalytic activity with sodium pyrophosphate and sodium phytate.
Alkaline Phosphatase Animals