Abstract
Procedures are described for the heterologous expression and purification of the mitochondrial-bound enzymes human and rat monoamine oxidases A and B and zebrafish MAO in the yeast Pichia pastoris. Enzyme expression is under control of a methanol oxidase promoter and similar procedures have been developed for the preparation of membrane particles and detergent solubilization of the functional enzymes. Similarities and differences are described in the procedures for purification of the respective enzymes using standard column chromatographic techniques to provide enzyme yields in the range of 100-300mg from 1L of cell culture.
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