title: Purification and properties of an acid phosphatase from lactating bovine mammary gland.
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.
authors.affiliation: Eastern Regional Research Center, United States Department of Agriculture, Philadelphia, PA 19118.
authors.forename: E W
authors.initials: EW
authors.lastname: Bingham
authors.forename: K
authors.initials: K
authors.lastname: Garver
mesh_terms: D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002417:Cattle / Q000378:metabolism*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology; D005260:Female; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007774:Lactation / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000135:Acid Phosphatase