FLUORIDE ACTIVATION OF RAT-BRAIN ADENYLATE-CYCLASE - REQUIREMENT FOR A PROTEIN COFACTOR

  • 1 January 1977
    • journal article
    • research article
    • Vol. 3  (2) , 119-128
Abstract
Activation of particulate adenylate cyclase and detergent-soluble (Lubrol PX) adenylate cyclase occurred when the enzyme was preincubated at 37.degree. C in the presence of 5 mM NaF and 5 mM MgSO4. Under these conditions the specific activity of the enzyme increased more than 2-fold in 8-12 min. Activation also occurred in the presence of 5 mM NaF alone, but the rate of activation was slower. Under these conditions, activation was inhibited by 1 mM EDTA, but this inhibition was prevented by Mg2+. No activation was observed at 0.degree. or in the absence of F. After repeated extraction with detergent, particulate adenylate cyclase was not stimulated by 5 mM NaF, and activation by preincubation with Mg2+ and F- was significantly reduced. Activation was restored by recombination of this particulate fraction with the initial detergent extract. This activating effect appeared to be mediated by 1 or more proteins present in the detergent extract.

This publication has 2 references indexed in Scilit: