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The Formation of , 1 4 Glucan from UDP--D-Glucose Catalyzed by a Phaseolus aureus Enzyme ¹

^a Department of Chemistry, Ohio University, Athens, Ohio 45701

Particulate enzyme preparations from Phaseolus aureus hypocotyls catalyze the formation of an alkali insoluble , 1 4 linked [¹⁴C]-glucan using UDP--D [¹⁴C]-glucose as substrate. Particulate enzymes prepared from root tissue also catalyzed the production of , 1 4 glucan. UDP--D-[¹⁴C]-glucose would not serve as a substrate for these enzymes. The presence or absence of , 1 4 glucan synthetase activity was independent of tissue source, substrate concentration, or homogenization method.

The particulate enzyme also catalyzes the formation of a , 1 3 linked glucan from UDP-D glucose which is usually soluble in hot alkali. The solubility of the , 1 3[¹⁴C]-glucan decreased when the enzyme was obtained from hypocotyls germinated at a higher temperature. The water-soluble material resulting from the catalyzed reaction includes a large proportion of what appears to be [¹⁴C]-laminaribiose, and smaller proportions of [¹⁴C]-laminaritriose and [¹⁴C]-glucose. There is no detectable quantity of [¹⁴C]-cellobiose or [¹⁴C]-cellotriose in the water-soluble material.