Effect of phospholipids on beef heart mitochondrial monoamine oxidase

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Abstract

Monoamine oxidase (monoamine: O2 oxidoreductase (deaminating), EC 1.4.3.4) was solubilized from beef heart mitochondria by sonication in the presence of substrate and Lubrol wx, and partially purified by chromatography on DEAE-cellulose and hydroxyapatite. Then, the enzyme preparation was applied to affinity chromatography using ω-aminohexyl agarose, and eluted successively with benzylamine and 5-hydroxytryptamine. The fraction eluted with 5-hydroxytryptamine had a higher specific activity on substrates for type A, 5-hydroxytryptamine, adrenaline, and noradrenaline, than on substrates for type B, benzylamine and β-phenethylamine. The fraction obtained with benzylamine as effluent had a higher specific activity on substrates for type B than on substrates for type A. Both fractions showed a single band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and molecular weight of the subunit was estimated to be 28,000. They contain a large amount of phospholipids (phosphatidylcholine, phosphatidylethanolamine, and lysophosphatidylcholine), glycerides, and cholesterol. The amounts of phospholipids were different in both fractions, though the ratios of the phospholipids were similar. By depletion of lipids from the enzyme preparation, the enzymatic activity was reduced markedly, but it could be restored by incorporation of the lipid-depleted enzyme into liposomes. These results indicate that lipid environment influences catalytic activity and substrate specificity of this oxidase.

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