Abstract
The effects of lipid degradation on proteins of smooth microsomal membranes isolated from young bean cotyledons have been examined by three techniques, viz. fluorescence energy transfer from tryptophan to cis-parinaric acid; protein spin-labelling with 3-maleimido PROXYL; and SDS-PAGE. Lipid degradation was induced in isolated membranes by activiting phospholipase D and phosphatidic acid phosphatase through the addition of Ca 2+ , by treatment with exogenous phospholipase C to simulate the concerted actions of phospholipase D and phosphatidic acid phosphatase or by treatment with exogenous phospholipase A 2 to generate endogenous substrate for lipoxygenase. All of the treatments induced time-dependent changes in lipid-protein interaction and in protein conformation, and the treatment with phospholipase A 2 also engendered proteolysis
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