ACID-PHOSPHATASE OF YEAST RHODOTORULA-RUBRA - PURIFICATION AND PROPERTIES OF ENZYME

  • 1 January 1977
    • journal article
    • research article
    • Vol. 24  (2) , 153-162
Abstract
Acid phosphatase from the yeast R. rubra was purified 44-fold. The purification procedure involved mechanical disruption of cells, precipitation with ethanol, chromatography on DEAE- and CM[carboxymethyl]-cellulose. The purified enzyme is homogeneous in polyacrylamide gel at pH 4.5, 9.5 and 8.4. Carbohydrate content accounts for 57% of the total weight. The optimum pH is at 4.0-4.6 and the enzyme is stable over pH range from 2.6-6.0. Full activity was retained on 60 min incubation at 50.degree. C, but it was reduced by half on 60 min incubation at 65.degree. C. Specificity of the enzyme is farily broad; monoesters of carbohydrates, nucleosides and PPi can serve as substrates. Km was found to be 1 .times. 10-4 M for p-nitrophenyl phosphate as a substrate. The enzyme is inhibited by molybdate, phosphate, arsenate and fluoride ions.

This publication has 2 references indexed in Scilit: