The aldehyde oxidase of the potato

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Abstract
Aldehyde oxidase was obtained by squeezing the juice from freshly minced potatoes. This juice strained through linen cloth was saturated with (NH4)2S04 and the precipitate filtered under suction. After washing several times with a saturated solution of (NH4)2SO4, the residue was dissolved in distilled water and filtered. The clear brown liquid thus obtained was repeatedly treated with Merck''s charcoal. The resulting solution was light brown and no less active than the untreated solution but contains only 10% of its original protein. The aldehyde oxidase contained in this solution will reduce NaNO3 to nitrite in the presence of acetaldehyde and other aldehydes. Other II acceptors than nitrate can be used, e.g., methylene blue, the Clark indicators, quinone, and m-dinitrobenzene. O may or may not act as a H acceptor. The activity of the enzyme varies according to the substances to be reduced, being much more restricted for methylene blue than for nitrate. Other precipitants were tried but all except the Pb salts proved poisonous. The activity of the enzyme is independent of traces of Fe.

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