The invertase of Tropaeolum majus leaves was partially purified. Its optimum pH was ca 5.25 and i... more The invertase of Tropaeolum majus leaves was partially purified. Its optimum pH was ca 5.25 and its K, values for sucrose, raffinose, and stachyose were 5.3, 17 and 25 mM respectively. The products of the reaction were in uitro inhibitors of the enzyme. Fructose was a partial competitive inhibitor (K, 49 mM) and glucose was a noncompetitive classical inhibitor (K, 57 mM). Proteins were activators of the enzyme. As activation by proteins suppressed the inhibitory effects of the reaction products, product inhibition does not appear to be involved in the physiological regulation of the enzyme.
The invertase of Tropaeolum majus leaves was partially purified. Its optimum pH was ca 5.25 and i... more The invertase of Tropaeolum majus leaves was partially purified. Its optimum pH was ca 5.25 and its K, values for sucrose, raffinose, and stachyose were 5.3, 17 and 25 mM respectively. The products of the reaction were in uitro inhibitors of the enzyme. Fructose was a partial competitive inhibitor (K, 49 mM) and glucose was a noncompetitive classical inhibitor (K, 57 mM). Proteins were activators of the enzyme. As activation by proteins suppressed the inhibitory effects of the reaction products, product inhibition does not appear to be involved in the physiological regulation of the enzyme.
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