Abstract
Ammonium sulfate fractions of supernatants from Physarum polycephalum browned rapidly at room temp. This browning was accompanied by complete inactivation of glutamate decarboxylase. Fractions exhibiting low activity and poor yields were obtained by decreasing plasmodium-buffer ratios of homogenates. Total activity of these fractions was increased by gel-filtration with Sephadex G-150. Samples of a crude slime mold pigment preparation inhibited supernatant activity by 42%. Since the enzyme was being inactivated either by phenols or their oxidation products, EDTA, cysteine, and Polyclar AT were added to extracting media to increase enzyme recovery. With their aid the enzyme was purified more than 15-fold by ammonium sulfate fractionation and gel-filtration with Sephadex G-200.
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