Summary: Non-specific acid phosphatase from cells was purified 111-fold by chromatography on DEAE-cellulose and gel filtration on Sephadex G-100 and Sepharose 4B. The enzyme is a glycoprotein containing 67% neutral sugars. The molecular mass of the highly purified acid phosphatase was found to be approximately 95 kDa by both SDS-PAGE and gel filtration. The pH and temperature optima were 5·8 and 55 °C, respectively. The enzyme was stable at pH values between 3·5 and 5·5 and at temperatures up to 60 °C. The purified phosphatase had a value of 3·64 mM for -nitrophenyl phosphate and showed broad substrate specificity.


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