Phosphoprotein Phosphatase in the Rat.

Abstract
Phosphoprotein phosphatase, (I) a specific enzyme, liberated inorganic P from casein and other phosphoproteins. A method of assay based on isolation of the liberated phosphate before the estimation, assured reproducible results. The pH optimum was around pH 5.8 with good stability at pH 5.8-7.0. I was inactivated 50% after 2 min. at 56[degree]. The temp. coeff. was 1.70 t 0.09. A study of a large number of inhibitors was made. I was found to be distributed widely in the body, with the highest activity in the spleen and liver.