Abstract
Cucumber (Cucumis sativus L.) cotyledons, a plant model system for studying changes in metabolic compartmentation, contain at least six forms of lipoxygenase. The intracellular location and organellar topology of lipoxygenase forms in lipid bodies, microsomes, and cytosol were investigated. A protocol was worked out to solubilize and prepare lipid-body lipoxygenase in an enzymatically active form. The methodology required for the solubilization of the lipid-body form differed from the procedure applicable for solubilization of two lipoxygenase forms from the microsomal membranes. Three cytosolic lipoxygenases were purified and found to be distinguishable from each other in size and charge. Further characterization and differentiation of all cellular lipoxygenase isoforms was achieved by comparison of the enzymatic properties. Marked differences in pH optima of the particle-bound lipoxygenases were found: optimal pH of 8.5 for lipid-body lipoxygenase and pH 5.5 for the microsomal lipoxygenases. In addition, analysis of the products formed showed that the catalytic properties of lipidbody lipoxygenase and microsomal lipoxygenase are clearly distinguishable from each other and from the soluble forms.
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