Abstract
Human placental acid phosohatase III has been purified 5000-fold from the crude tissue homogenate by a combination of gel filtration and ion-exchange chromatography. The resultant material had a specific activity of 10 international units p-nitrophenyl phosphate phosphatase activity per mg protein at 37°, and a pH optimum of 5.2–5.3 in sodium citrate. In sodium acetate buffer the pH curve was flattened and its optimum shifted to pH 4.8–5.0. Addition of 6-ethylmercaptopurine to the reaction mixture greatly stimulated the hydrolysis of p-nitrophenyl phosphate without further changing the pH curve. Purified enzyme III is moderately sensitive to gluteraldehyde and extremely sensitive to inactivation by heavy metal ions. These and other physico chemical properties of this enzyme are discussed in relation to difficulties in its histochemical visualization, possible uniqueness in human tissue, and similarities to an enzyme found in rabbit heterophil leukocytes.
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