Susceptibility of UDP-Glucose:(1,3)-beta-Glucan Synthase to Inactivation by Phospholipases and Trypsin.
UDP-glucose:(1,3)-beta-glucan synthase from Beta vulgaris L. was rapidly inactivated by treatment with phospholipases C, D, and A(2). 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.
Sloan
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ME
Department of Food Science, New Jersey Agricultural Experiment Station, Cook College, Rutgers University, New Brunswick, New Jersey 08903.
Wasserman
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BP