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

Margaret E. Sloan | Zendy; Bruce P. Wasserman | Zendy

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

Author(s) -

Margaret E. Sloan,

Bruce P. Wasserman

Publication year - 1989

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.89.4.1341

Subject(s) - divalent , phosphatidylethanolamine , chemistry , biochemistry , enzyme , trypsin , phospholipase , atp synthase , phospholipase a , phospholipase a2 , membrane , phospholipid , phosphatidylcholine , organic chemistry

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.

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