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. 1989 Apr;89(4):1341–1344. doi: 10.1104/pp.89.4.1341

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

Margaret E Sloan 1,2, Bruce P Wasserman 1
PMCID: PMC1056019  PMID: 16666707

Abstract

UDP-glucose:(1,3)-β-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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