PURIFICATION AND SOME PROPERTIES OF THE MAIN POLYMORPHIC FORM OF ACID-PHOSPHATASE FROM POA-PRATENSIS SEEDS

  • 1 January 1980
    • journal article
    • research article
    • Vol. 27  (3-4) , 345-352
Abstract
The main polymorphic form of acid phosphatase was isolated from P. pratensis seeds by chromatography on DEAE and CM cellulose and gel filtration on Bio-Gel P-100. The enzyme migrated as a single band in disc electrophoresis at pH 4.5 and 8.4. The purified enzyme is a glycoprotein of MW .apprx. 33,000. Carbohydrate content accounts for 40% of the total weight. The optimum pH is at 5.2 and the apparent Km for p-nitrophenylphosphate is 0.55 mM. Fluoride ions are noncompetitive and Zn ions, uncompetitive inhibitors, with apparent Km values of 0.55 and 0.28 mM, respectively.