ACTIVATION OF ACID PROSTATE PHOSPHATASE BY 1-PENTANOL

  • 1 January 1976
    • journal article
    • research article
    • Vol. 14  (12) , 581-587
Abstract
The activity of the acid phosphatase [EC 3.1.3.2] [human] from prostate was increased by 90% by the addition of 150 mM 1-pentanol to the assay mixture. This activation results in an increased turnover of substrate, so that the phosphomonoester is cleaved more rapidly and a correspondingly larger amount of the released organic residue can be detected. The quantity of free phosphate does not correspond to the substrate turnover, because some of the phosphate residue is transferred from the substrate to the 1-pentanol in a transphosphorylation reaction. The influence of the substrate, buffer, pH and tartrate on the 1-pentanol-activated prostate phosphatase was investigated.