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Metabolism and Enzymology

Susceptibility of UDP-Glucose:(1,3)--Glucan Synthase to Inactivation by Phospholipases and Trypsin ¹

Department of Food Science, New Jersey Agricultural Experiment Station, Cook College, Rutgers University, New Brunswick, New Jersey 08903

UDP-glucose:(1,3)--glucan synthase from Beta vulgaris L. was rapidly inactivated by treatment with phospholipases C, D, and A₂. Enzyme activity could not be restored to the phospholipase-treated enzyme by the addition of phosphatidylethanolamine or other phospholipids. Membrane-bound and solubilized glucan synthase were also trypsin-labile with inactivation rates equal in the presence or absence of divalent cations or chelators. Gradual activity declines were observed in membranes incubated with divalent cations, but not with chelators.

¹ This research was supported in part by grants DMD 85-02523 from the National Science Foundation, 87-CRCR-1-2414 from the U.S. Department of Agriculture, the Charles and Johanna Busch Foundation, and the New Jersey Agricultural Experiment Station with State and Hatch Act Funds. New Jersey Agricultural Experiment Station Publication No. D-10546-2-88.