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  • Title: Purification and properties of an acid phosphatase from lactating bovine mammary gland.
    Author: Bingham EW, Garver K.
    Journal: J Dairy Sci; 1990 Apr; 73(4):964-9. PubMed ID: 2345206.
    Abstract:
    An acid phosphatase was partially purified from the cytosol of lactating bovine mammary gland by precipitation with ammonium sulfate and protamine, chromatography on carboxymethyl cellulose, and gel filtration on Sephadex G-75. The enzyme hydrolyzed aromatic phosphates but was less active toward alkyl phosphates, ATP, and phosphoproteins (casein and phosvitin). A sulfhydryl group seems to be essential for activity, since dithiothreitol and cysteine activated the enzyme; compounds that react with the sulphydryl groups in proteins were inhibitory. Orthovanadate, phosphate, and zinc ions also inhibited the phosphatase.
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