The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme.

The enzyme oxidizing cysteamine to hypotaurine has been extracted from horse kidney and purified. The final product behaves as a single protein when analyzed in the ultracentrifuge, by starch gel electrophoresis, and by filtration on dextran gels. The sedimentation coefficient of the pure product is s20, w = 5.9. The molecular weight determined by the Yphantis procedure (22) is 83,000. Nonheme iron is contained in the amount of 1 atom per molecule of enzyme. Spectrophoto-metric analyses indicate absence of nonprotein chromophores in the visible and in the near ultraviolet range. The complete amino acid composition has been determined by ion exchange chromatography. The effect of sulfide, methylene blue, and hydroxylamine, which act as cofactor-like compounds, has been studied. Of the substrates assayed (cysteamine, cysteine, cysteine ethyl and methyl esters, and reduced glutathione), only cysteamine is oxidized to the sulfinic derivative in the presence of the cofactor-like compounds named