Abstract
UDP-glucose dehydrogenase was partially purified from germinating lily pollen ( Lilium longiflorum). The enzyme was associated with the particulate fraction in extracts of nongerminated pollen but could be solubilized when this fraction was treated with the detergent Tween 80. The enzyme was inhibited by UDP-galacturonic acid, UDP-glucuronic acid, and UDP-xylose. The latter was a powerful inhibitor when concentration of the substrate UDP-glucose was low and caused the normally hyperbolic UDP-glucose saturation curve to become sigmoid. These data were interpreted as indicating cooperative effects, UDP-glucose dehydrogenase being viewed as a regulatory enzyme.
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