A homogeneous sample of lipoxygenase from rabbit reticulocyte cytosol was obtained. The rate of exogenous arachidonate oxidation by reticulocyte lipoxygenase was found to increase in the presence of various blood plasma lipoproteins of mammals. The rate of arachidonate oxidation by soybean lipoxygenase in the presence of these lipoproteins was either unaffected or decreased. The lipoproteins immobilized the substrate; however, preliminary "saturation" of the lipoproteins by a manyfold excess of non-oxidizable oleate did not eliminate the enzyme activation by the lipoproteins. It was concluded that lipoxygenase activation is due to conformational changes of the enzyme during its interaction with membrane components.
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