Susceptibility of UDP-Glucose:(1,3)-β-Glucan Synthase to Inactivation by Phospholipases and Trypsin
- 1 April 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 89 (4) , 1341-1344
- https://doi.org/10.1104/pp.89.4.1341
Abstract
UDP-glucose:(1,3)-.beta.-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.This publication has 17 references indexed in Scilit:
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