Electrophoretic studies on cytochrome oxidase

A modified preparation of cytochrome oxidase has been described. The preparation is extremely low in contaminating hemoproteins. Because it required only a low salt concentration for solubility, it was suitable for electrophoretic studies. Paper electrophoresis resulted in the separation of two fluorescent and three hemoprotein areas. Employing a spray reagent which contained a leuco dye and cytochrome c, it was possible to locate active cytochrome oxidase in only one area of the paper. Column electrophoresis of the preparation showed that at least partial separation of the hemoprotein having cytochrome oxidase activity from inactive hemoprotein had occurred. Both hemoproteins fractions exhibited the spectral properties of cytochromes α and α 3, and the ratio of these cytochromes was uniform throughout.