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The effect of salts on a - glucan phosphorylase activity



The effect of salts on a - glucan phosphorylase activity



Prikladnaya Biokhim Mikrobiol 1(2): 206-211



The addition of 0. 001 [image] (NH4) 2SO4 or MgSO4 increased the synthetic activity of purified preparations of glucan phosphorylase from potato tubers. The addition of 0. 001[image] and 0. 1 [image] KNO3, K2SO4 and Na2SO4 separately did not produce regular and substantial changes in the activity of this enzyme. In the presence of 0. 001 [image] MgSO4 the K2SO4, Na2SO4 and (NH4) 2SO4 at a concentration of 0. 1 [image] increased the enzymatic activity of purified glucan phosphorylase. Since different cations and anions had roughly the same effect, it may be conjectured that the observed activation is not of a specific character, but is associated with the physical-chemical properties of the protein part of the enzyme. In the presence of 0. 001 [image] MgSO4, the K2SO4, Na2SO4, and (NH4) 2SO4 in concentrations of 0. 1 [image] reduced somewhat the synthetic activity of [alpha]-glucan phosphorylase. Since nitration under these conditions did not have an inhibiting effect, and since inhibition was maximal for (NH4) 2SO4 among the sulfates studied, it may be conjectured that the observed reduction of enzyme activity is connected with the dehydrating, salting-out effect of the sulfate salts on the enzyme protein. When 0. 01 [image] NH4NO3 or NH4SO4 was added to plant tissue homogenates, [alpha]-glucan phosphorylase activity increased; an inhibiting effect was observed only in the presence of 1 [image] concentrations. In both cases the effective concentrations were one order of magnitude higher than in experiments with purified enzyme preparations.

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