Hartmannella culbertsoni: enzymatic, ultrastructural, and cytochemical characteristics of peroxisomes in a density gradient |
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Authors: | G E Childs |
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Institution: | Department of Tropical Medicine and Medical Parasitology, Louisiana State University Medical Center, New Orleans, Louisiana 70112 U.S.A. |
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Abstract: | Isopycnic density gradient centrifugation techniques demonstrated that catalase (EC 1.11.1.6) and urate oxidase (EC 1.7.3.3) had similar distribution patterns with a peak at equilibrium density 1.22 suggesting that both enzymes were associated with a single population of subcellular particles. Catalase (EC 1.11.1.6) was shown cytochemically to be associated with peroxisomes in the sediment of the catalase-rich fractions. Protein showed a bimodal distribution with a soluble peak at density 1.10 and a particulate peak at density 1.20. The particulate protein peak corresponded to the mitochondrial peak. Acid phosphatase (EC 3.1.3.2) had an equilibrium density of 1.10. Acid phosphatase (EC 3.1.3.2) localization and ultrastructural examination of the acid phosphatase-rich fraction revealed that activity was associated with vacuoles. No primary lysosomes were identified. |
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Keywords: | Catalase (EC 1 11 1 6) Urate oxidase (EC 1 7 3 3) Acid phosphatase (EC 3 1 3 2) Peroxisomes Lysosomes Enzymes Electron microscopy Density gradient centrifugation EC 1 11 1 6 (catalase) EC 1 7 3 3 (urate oxidase) EC 3 1 3 2 (acid phosphatase) Malate dehydrogenase (EC 1 1 1 37) EC 1 1 1 37 (malate dehydrogenase) |
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