Immunological and Electrophoretic Analysis of the Alternative Oxidase of Arum Maculatum Sub-Mitochondrial Particles

Abstract

Solubilization and partial purification of the alternative (quinol) oxidase of mitochondria isolated from spadices of Arum maculatum has been described several times^1–3. Failure to further purify the oxidase has led to other suggestions regarding the nature of SHAM sensitive quinol oxidation in plant mitochondria, such as non-enzymic lipid peroxidation⁴. Recently a comprehensive purification using ammonium acetate precipitation and sucrose density gradient centrifugation resulted in a preparation of increased activity, similar inhibitor sensitivities and significant iron content. SDS-PAGE of the preparation reveals a major band of molecular weight 34KD however a number of other bands are still present⁵.