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- W2169571849 abstract "Particulate enzyme preparations from Phaseolus aureus hypocotyls catalyze the formation of an alkali insoluble β, 1 → 4 linked [14C]-glucan using UDP-α-d [14C]-glucose as substrate. Particulate enzymes prepared from root tissue also catalyzed the production of β, 1 → 4 glucan. UDP-β-d-[14C]-glucose would not serve as a substrate for these enzymes. The presence or absence of β, 1 → 4 glucan synthetase activity was independent of tissue source, substrate concentration, or homogenization method. The particulate enzyme also catalyzes the formation of a β, 1 → 3 linked glucan from UDP-d glucose which is usually soluble in hot alkali. The solubility of the β, 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." @default.
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- W2169571849 date "1972-09-01" @default.
- W2169571849 modified "2023-09-26" @default.
- W2169571849 title "The Formation of β, 1 → 4 Glucan from UDP-α-d-Glucose Catalyzed by a <i>Phaseolus aureus</i> Enzyme" @default.
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- W2169571849 doi "https://doi.org/10.1104/pp.50.3.371" @default.
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